454:
557:
2795:
29:
545:
594:. Upon ATP binding in this pocket, it is believed that a conformational change occurs allowing the rotation of the CA domain to come into contact with the DHp of the other monomer and thus allowing the conserved His-260 to rest near the γ phosphate. The Nε of His-260 then attacks the γ phosphate of ATP in a
585:
The final side of the ATP binding pocket is conveniently named the “ATP lid.” The stability of this structure is mediated by the presence of the γ phosphate and thus the Mg ion in the binding site. Also the presence of the nucleotide base has proved to play a significant role in stabilization of the
517:
and is formed by residues 232-317. The histidine phosphorylation site is located at His-260. The N, G1, F and G2 boxes are contained in the C-terminal catalytic and ATP-binding (CA) domain. This domain is formed by residues 323-489 and forms a structure known as an α/β sandwich fold. This particular
577:
amine group. Three other water molecules form direct hydrogen bonds with the adenine base. A Mg ion forms a bridge between all three phosphates and an invariant Asn residue. Finally, two more water molecules complete octahedral coordination with Mg and are linked to Arg-408 and His-405. When the Îł
572:
binding pocket is contained within the CA domain and the structural similarity of this pocket is high between most HKs. The cavity of CheA, also crystallized from T. maritima, is first formed by β sheet P4 in the rear and the sides of the cavity are formed by the 4 motifs mentioned earlier, the N,
338:
protein (or sometimes on the kinase itself). More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells. In marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated
498:
cytoplasmic catalytic domain. HKs are known to serve roles in many different signal transduction pathways, so it is not surprising that the extracellular sensing domain is not very well conserved in the HK family. In contrast, the cytoplasmic domain tends to have high sequence
339:
Histidine using standard biochemical and mass spectrometric approaches is much more challenging, and special procedures and separation techniques are required for their preservation alongside classical Ser, Thr and Tyr phosphorylation on proteins isolated from human cells.
664:
was reported to use SrrAB TCSs consisting of a sensor HKs (SrrB), which would transfer phosphate group to an effector response regulator (SrrA), leading to the modification of SrrA activity including gene regulation. This TCSs has been used by
931:
Hardman G, Perkins S, Ruan Z, Kannan N, Brownridge P, Byrne DP, Eyers PA, Jones AR, Eyers CE (13 October 2017). "Extensive non-canonical phosphorylation in human cells revealed using strong-anion exchange-mediated phosphoproteomics".
578:
phosphate of ATP is destabilized, the Mg is no longer observed due to its inability to octahedrally coordinate. Marina et al. argue that similar coordination of Mg occurs in HK853 but that it is unobserved due to the usage of the ATP
2322:
473:
unit may rotate in such a way that the ATP binding pocket of that unit can come into contact with a particular histidine residue on the opposite unit and a nucleophilic addition results in a phosphorylated histidine.
573:
G1, F, and G2 boxes. The majority of the residues coming from the β sheet are hydrophobic with Asp449 being the exception. This residue is invariant and forms a hydrogen bond along with a water molecule to the
1192:
Kowluru A (2002). "Identification and characterization of a novel protein histidine kinase in the islet beta cell: evidence for its regulation by mastoparan, an activator of G-proteins and insulin secretion".
507:. These motifs include the H, N, G1, F, and G2 boxes. The autophosphorylation H-box is contained in the N-terminal dimerization and histidine phosphotransfer (DHp) domain. In HK853-CD, crystallized from
1501:
Hirschman A, Boukhvalova M, VanBruggen R, Wolfe AJ, Stewart RC (November 2001). "Active site mutations in CheA, the signal-transducing protein kinase of the chemotaxis system in
Escherichia coli".
1222:
Yoshimi A, Tsuda M, Tanaka C (2004). "Cloning and characterization of the histidine kinase gene Dic1 from
Cochliobolus heterostrophus that confers dicarboximide resistance and osmotic adaptation".
529:
manner with both α2 helices. The stability of the dimer is aided by several interactions at the interface between the DHps of each monomer. These include hydrophobic interactions between conserved
2332:
2327:
416:
2447:
2425:
2243:
445:
This type of enzyme is involved in signal transduction pathways upstream of many cellular processes including various metabolic, virulence, and homeostatic pathways.
207:
1085:"Deletion of the Two-Component Histidine Kinase Gene (CHK1) of Candida albicans Contributes to Enhanced Growth Inhibition and Killing by Human Neutrophils In Vitro"
469:
The mechanism for the reactions catalyzed by histidine kinase have not been completely elucidated, but current evidence suggests that the catalytic domain of one
226:
896:
Gonzalez-Sanchez MB, Lanucara F, Helm M, Eyers CE (2013). "Attempting to rewrite
History: challenges with the analysis of histidine-phosphorylated peptides".
541:(Lys-270Glu-303’). Further interactions are mediated via hydrogen bonds to water within a cavity inside the coiled coil and flanked by hydrophobic residues.
2353:
2248:
2415:
525:
The dimeric unit is held together by a four-helix bundle, formed when the C-terminal segments of the α1 helices on each subunit interact in an
2054:
790:
Fuhs SR, Meisenhelder J, Aslanian A, Ma L, Zagorska A, Stankova M, Binnie A, Al-Obeidi F, Mauger J, Lemke G, Yates JR 3rd, Hunter T (2015).
2820:
1460:"Cys303 in the Histidine Kinase PhoR Is Crucial for the Phosphotransfer Reaction in the PhoPR Two-Component System in Bacillus subtilis"
590:. The ATP lid is connected via hydrophobic residues to the rest of the protein. The Îł phosphate of ATP is somewhat exposed allowing for
2188:
2514:
1758:
1552:
1899:
219:
669:
in order to sense changes of environmental condition and transmit the signal to an appropriate responding system, for example,
611:
327:
170:
146:
2670:
2472:
2467:
2027:
1845:
560:
Structure and environment of HK853 ATP binding pocket. Important residues are labeled and red spheres are water molecules.
2785:
2337:
2225:
2193:
2178:
1415:
Ryan L. Brunsing; Chandra La Clair; Sharon Tang; Christina Chiang; Lynn E. Hancock; Marta Perego; James A Hoch (2005).
1860:
526:
1040:
Bilwes AM, Quezada CM, Croal LR, Crane BR, Simon MI (April 2001). "Nucleotide binding by the histidine kinase CheA".
660:
Similar to fungus, Two component systems can also be found in several persistent bacteria infections. For example,
582:
AMPPNP in the crystal structure. During crystallization, the analog was hydrolyzed into a product similar to ADP.
322:
or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of
294:(RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell (
2655:
2771:
2758:
2745:
2732:
2719:
2706:
2693:
2458:
2436:
2411:
2386:
2306:
1914:
1874:
1819:
1796:
1768:
1736:
1602:
291:
2665:
1689:
164:
2619:
2562:
1923:
1904:
1835:
1569:
673:
genes is induced by SrrAB to mediate cell assembly and biofilm formation to survive under anaerobic condition.
587:
423:
347:
57:
151:
2567:
1781:
287:
2235:
2008:
1918:
641:
569:
427:
331:
401:
231:
2588:
2507:
2089:
2044:
1746:
1731:
1667:
1647:
1545:
599:
595:
439:
251:
139:
33:
2660:
334:
to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a
1530:
1132:
Tiwari N, LĂłpez-Redondo M, Miguel-Romero L, Kulhankova K, Cahill MP, Tran PM, et al. (May 2020).
74:
2003:
1998:
1878:
1741:
1721:
1630:
933:
852:
743:"pHisphorylation: the emergence of histidine phosphorylation as a reversible regulatory modification"
307:
2624:
2266:
2258:
2039:
1706:
1642:
1606:
509:
435:
267:
167:
69:
91:
2815:
2557:
2129:
2067:
2018:
1753:
1580:
1403:
1247:
1065:
615:
579:
335:
319:
279:
792:"Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation"
2144:
2134:
2124:
2049:
2033:
1992:
1978:
1973:
1711:
1674:
1518:
1489:
1446:
1395:
1360:
1325:
1290:
1239:
1210:
1169:
1114:
1057:
1022:
987:
913:
878:
821:
772:
723:
591:
500:
392:
158:
38:
1083:
Torosantucci A, Chiani P, De
Bernardis F, Cassone A, Calera JA, Calderone R (February 2002).
2603:
2598:
2572:
2500:
2139:
2119:
2061:
1957:
1855:
1840:
1786:
1684:
1679:
1538:
1510:
1479:
1471:
1436:
1428:
1385:
1350:
1339:"Identification of the site of phosphorylation on the osmosensor, EnvZ, of Escherichia coli"
1315:
1280:
1272:
1231:
1202:
1159:
1149:
1104:
1096:
1049:
1014:
977:
969:
905:
868:
860:
841:"Gas-phase intermolecular phosphate transfer within a phosphohistidine phosphopeptide dimer"
811:
803:
762:
754:
713:
703:
629:
620:
504:
453:
127:
2650:
2634:
2547:
2400:
2390:
2212:
2183:
1809:
1716:
1701:
1304:"Genetic evidence for histidine kinase HP165 being an acid sensor of Helicobacter pylori"
1005:
Parkinson JS, Kofoid EC (1992). "Communication modules in bacterial signaling proteins".
103:
1018:
856:
62:
2799:
2688:
2629:
2368:
2207:
2114:
2106:
1983:
1946:
1484:
1459:
1441:
1416:
1320:
1303:
1164:
1133:
982:
957:
873:
840:
816:
791:
767:
742:
483:
323:
202:
1390:
1373:
1355:
1338:
1285:
1260:
1206:
1109:
1084:
718:
691:
465:-nitrogen occurs through the other histidine tautomer. B = unspecified enzymatic base.
182:
2809:
2593:
2552:
1637:
1432:
708:
645:
637:
534:
490:
cytoplasmic portion connected to an extracellular sensing domain via a transmembrane
470:
311:
303:
295:
275:
271:
177:
1407:
1276:
1251:
1069:
318:
activity, the intracellular domains typically have regions that bind to a secondary
2542:
1726:
1696:
1625:
1100:
958:"Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein"
636:
with a deletion of CHK1, the two-component histidine kinase gene, show defects in
556:
2766:
2701:
2537:
2292:
2282:
1883:
1620:
1561:
649:
625:
538:
491:
283:
259:
186:
2794:
1142:
Proceedings of the
National Academy of Sciences of the United States of America
864:
807:
2094:
1937:
1850:
1615:
1565:
1235:
758:
692:"Histidine protein kinases: key signal transducers outside the animal kingdom"
565:
530:
519:
495:
487:
343:
1372:
Alexandrine M. Bilwes; Lisa A. Alex; Brian R. Crane; Melvin I. Simon (1999).
973:
2740:
2714:
2373:
2286:
1823:
1589:
1261:"Molecular Characterization of Two-Component Systems of Helicobacter pylori"
1154:
640:
and a drastic decrease in the cell’s ability to resist elimination by human
514:
431:
388:
1522:
1493:
1450:
1329:
1294:
1243:
1214:
1173:
1118:
1061:
991:
917:
882:
825:
776:
727:
1399:
1364:
1026:
494:. A second transmembrane α helix connects the extracellular domain to the
2220:
1800:
1417:"Characterization of Sporulation Histidine Kinases of Bacillus anthracis"
618:
protein, may be critical to the virulence of some fungal strains such as
457:
Proposed mechanism of histidine kinase, depicting phosphorylation of the
1475:
909:
644:. As humans lack this two-component system, it may be a good target for
350:
115:
2171:
2156:
1772:
574:
544:
299:
255:
134:
36:
structure of ATP:protein-L-histidine N-phosphotransferase based on the
1514:
42:
28:
2753:
2523:
2149:
1584:
384:
315:
263:
214:
110:
98:
86:
938:
2727:
2166:
2161:
2013:
1053:
555:
543:
452:
2323:
CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
2077:
2072:
1968:
1963:
1662:
1657:
1652:
122:
2496:
1534:
839:
Gonzalez-Sanchez MB, Lanucara F, Hardman GE, Eyers CE (2014).
371:
250:) are multifunctional, and in non-animal kingdoms, typically
314:
domain) that contain the enzymatic activity. In addition to
270:
across the cellular membrane. The vast majority of HKs are
2492:
1374:"Structure of CheA, a Signal-Transducing Histidine Kinase"
548:
Single monomer. Red residue is His-260, ligand (ADP and SO
956:
Marina A, Waldburger CD, Hendrickson WA (December 2005).
405:
306:-like molecules, portions that span the cell membrane (
2783:
2333:
CDP-diacylglycerol—inositol 3-phosphatidyltransferase
404:
2338:
CDP-diacylglycerol—choline O-phosphatidyltransferase
2679:
2643:
2612:
2581:
2530:
2457:
2435:
2410:
2385:
2366:
2346:
2328:
CDP-diacylglycerol—serine O-phosphatidyltransferase
2315:
2305:
2275:
2257:
2234:
2206:
2105:
1945:
1936:
1913:
1873:
1818:
1795:
1767:
1601:
1577:
225:
213:
201:
196:
176:
157:
145:
133:
121:
109:
97:
85:
80:
68:
56:
51:
21:
614:(TCSs), involving histidine kinase and a variable
410:
1138:pathogenicity through redox sensitive cysteines"
522:and the other layer is made of three α helices.
951:
949:
537:(Thr-252Glu-316’ and Arg-263Asn-307’) and one
290:for signaling molecules in a way analogous to
2508:
1546:
330:in which HK transfers a phosphate group from
16:Family of enzymes important in cell signaling
8:
1302:Pflock M, Dietz P, Schar J, Beier D (2004).
518:fold has one layer composed of a 5-stranded
328:two-component signal transduction mechanisms
2354:N-acetylglucosamine-1-phosphate transferase
2244:UTP—glucose-1-phosphate uridylyltransferase
2515:
2501:
2493:
2382:
2312:
1942:
1933:
1598:
1553:
1539:
1531:
1134:"The SrrAB two-component system regulates
690:Wolanin PW, Thomason PA, Stock JB (2002).
193:
27:
2448:serine/threonine-specific protein kinases
2426:serine/threonine-specific protein kinases
2249:Galactose-1-phosphate uridylyltransferase
1483:
1440:
1389:
1354:
1337:Roberts DL, Bennett DW, Forst SA (1994).
1319:
1284:
1163:
1153:
1108:
981:
937:
872:
815:
766:
717:
707:
624:, which is often responsible for causing
403:
2790:
682:
1458:Amr Eldakak; F. Marion Hulett (2007).
18:
7:
418:ADP + protein N-phospho-L-histidine.
1019:10.1146/annurev.ge.26.120192.000443
442:and protein N-phospho-L-histidine.
411:{\displaystyle \rightleftharpoons }
1321:10.1111/j.1574-6968.2004.tb09512.x
461:-nitrogen. Phosphorylation of the
14:
1759:Glucose-1,6-bisphosphate synthase
310:), and portions within the cell (
2793:
1900:Ribose-phosphate diphosphokinase
1433:10.1128/JB.187.20.6972-6981.2005
709:10.1186/gb-2002-3-10-reviews3013
552:) is yellow, ATP lid is magenta.
503:and contains several well-known
1277:10.1128/JB.182.8.2068-2076.2000
1:
2473:Protein-histidine tele-kinase
2468:Protein-histidine pros-kinase
2347:Glycosyl-1-phosphotransferase
1391:10.1016/S0092-8674(00)80966-6
1356:10.1016/S0021-9258(17)37029-1
1207:10.1016/S0006-2952(02)01025-0
1101:10.1128/IAI.70.2.985-987.2002
482:An HK is composed of several
326:, HKs are usually parts of a
2179:RNA-dependent RNA polymerase
702:(10): reviews3013.1–3013.8.
2086:RNA-directed DNA polymerase
1954:DNA-directed DNA polymerase
656:Role in bacteria infections
513:, this domain is a helical-
2837:
2821:Enzymes of known structure
2439:: protein-dual-specificity
865:10.1016/j.ijms.2014.04.015
808:10.1016/j.cell.2015.05.046
741:Fuhs SR, Hunter T (2017).
398:ATP + protein L-histidine
367:protein kinase (histidine)
2671:Michaelis–Menten kinetics
1259:Beier D, Frank R (2000).
1236:10.1007/s00438-003-0974-4
759:10.1016/j.ceb.2016.12.010
648:agents in order to treat
606:Role in fungal infections
292:tyrosine kinase receptors
286:activity. HKs can act as
192:
26:
2563:Diffusion-limited enzyme
2416:protein-serine/threonine
2316:Phosphatidyltransferases
1905:Thiamine diphosphokinase
974:10.1038/sj.emboj.7600886
533:residues as well as two
363:protein histidine kinase
359:histidine protein kinase
22:protein histidine kinase
1155:10.1073/pnas.1921307117
2236:Nucleotidyltransferase
1919:nucleotidyltransferase
1846:Nucleoside-diphosphate
602:as its leaving group.
561:
553:
486:starting with a short
478:Structure and function
466:
412:
346:, a histidine kinase (
2656:Eadie–Hofstee diagram
2589:Allosteric regulation
2090:Reverse transcriptase
1136:Staphylococcus aureus
662:Staphylococcus aureus
596:nucleophilic addition
559:
547:
456:
413:
298:domain) that bind to
2666:Lineweaver–Burk plot
1879:diphosphotransferase
1861:Thiamine-diphosphate
1568:-containing groups (
1308:FEMS Microbiol. Lett
1224:Mol. Genet. Genomics
612:two-component system
402:
308:transmembrane domain
266:that play a role in
46: coordinates.
2461:: protein-histidine
2379:; protein acceptor)
2267:mRNA capping enzyme
2259:Guanylyltransferase
1476:10.1128/JB.01205-06
1148:(20): 10989–10999.
910:10.1042/bst20130072
857:2014IJMSp.367...28G
845:Int J Mass Spectrom
747:Curr Opin Cell Biol
510:Thermotoga maritima
426:of this enzyme are
268:signal transduction
2625:Enzyme superfamily
2558:Enzyme promiscuity
1737:Phosphoinositide 3
1581:phosphotransferase
1195:Biochem. Pharmacol
616:response regulator
562:
554:
467:
434:, whereas its two
408:
336:response regulator
288:cellular receptors
2781:
2780:
2490:
2489:
2486:
2485:
2362:
2361:
2301:
2300:
2202:
2201:
2115:Template-directed
1869:
1868:
1836:Phosphomevalonate
1515:10.1021/bi0113622
1042:Nat. Struct. Biol
898:Biochem Soc Trans
630:immunocompromised
592:dephosphorylation
393:chemical reaction
320:effector molecule
244:Histidine kinases
241:
240:
237:
236:
140:metabolic pathway
2828:
2798:
2797:
2789:
2661:Hanes–Woolf plot
2604:Enzyme activator
2599:Enzyme inhibitor
2573:Enzyme catalysis
2517:
2510:
2503:
2494:
2478:Histidine kinase
2401:tyrosine kinases
2391:protein-tyrosine
2383:
2313:
2120:RNA polymerase I
1943:
1934:
1787:Aspartate kinase
1782:Phosphoglycerate
1599:
1555:
1548:
1541:
1532:
1526:
1509:(46): 13876–87.
1497:
1487:
1454:
1444:
1411:
1393:
1368:
1358:
1333:
1323:
1298:
1288:
1255:
1218:
1201:(12): 2091–100.
1178:
1177:
1167:
1157:
1129:
1123:
1122:
1112:
1080:
1074:
1073:
1037:
1031:
1030:
1007:Annu. Rev. Genet
1002:
996:
995:
985:
953:
944:
943:
941:
928:
922:
921:
904:(4): 1089–1095.
893:
887:
886:
876:
836:
830:
829:
819:
787:
781:
780:
770:
738:
732:
731:
721:
711:
687:
621:Candida albicans
586:lid in a closed
417:
415:
414:
409:
194:
45:
34:Crystallographic
31:
19:
2836:
2835:
2831:
2830:
2829:
2827:
2826:
2825:
2806:
2805:
2804:
2792:
2784:
2782:
2777:
2689:Oxidoreductases
2675:
2651:Enzyme kinetics
2639:
2635:List of enzymes
2608:
2577:
2548:Catalytic triad
2526:
2521:
2491:
2482:
2453:
2431:
2406:
2377:
2371:
2367:2.7.10-2.7.13:
2358:
2342:
2309:: miscellaneous
2297:
2271:
2253:
2230:
2213:exoribonuclease
2210:
2198:
2184:Polyadenylation
2101:
1927:
1921:
1909:
1891:
1887:
1881:
1865:
1827:
1814:
1791:
1763:
1593:
1587:
1579:
1573:
1559:
1529:
1500:
1457:
1427:(20): 6972–81.
1414:
1371:
1349:(12): 8728–33.
1336:
1301:
1258:
1221:
1191:
1187:
1185:Further reading
1182:
1181:
1131:
1130:
1126:
1082:
1081:
1077:
1039:
1038:
1034:
1004:
1003:
999:
968:(24): 4247–59.
955:
954:
947:
930:
929:
925:
895:
894:
890:
838:
837:
833:
789:
788:
784:
740:
739:
735:
689:
688:
684:
679:
658:
608:
551:
480:
451:
400:
399:
324:protein kinases
280:phosphotransfer
47:
37:
17:
12:
11:
5:
2834:
2832:
2824:
2823:
2818:
2808:
2807:
2803:
2802:
2779:
2778:
2776:
2775:
2762:
2749:
2736:
2723:
2710:
2697:
2683:
2681:
2677:
2676:
2674:
2673:
2668:
2663:
2658:
2653:
2647:
2645:
2641:
2640:
2638:
2637:
2632:
2627:
2622:
2616:
2614:
2613:Classification
2610:
2609:
2607:
2606:
2601:
2596:
2591:
2585:
2583:
2579:
2578:
2576:
2575:
2570:
2565:
2560:
2555:
2550:
2545:
2540:
2534:
2532:
2528:
2527:
2522:
2520:
2519:
2512:
2505:
2497:
2488:
2487:
2484:
2483:
2481:
2480:
2475:
2470:
2464:
2462:
2455:
2454:
2452:
2451:
2442:
2440:
2433:
2432:
2430:
2429:
2420:
2418:
2408:
2407:
2405:
2404:
2395:
2393:
2380:
2375:
2369:protein kinase
2364:
2363:
2360:
2359:
2357:
2356:
2350:
2348:
2344:
2343:
2341:
2340:
2335:
2330:
2325:
2319:
2317:
2310:
2303:
2302:
2299:
2298:
2296:
2295:
2290:
2279:
2277:
2273:
2272:
2270:
2269:
2263:
2261:
2255:
2254:
2252:
2251:
2246:
2240:
2238:
2232:
2231:
2229:
2228:
2223:
2217:
2215:
2208:Phosphorolytic
2204:
2203:
2200:
2199:
2197:
2196:
2191:
2186:
2181:
2176:
2175:
2174:
2169:
2164:
2154:
2153:
2152:
2142:
2137:
2132:
2127:
2122:
2117:
2111:
2109:
2107:RNA polymerase
2103:
2102:
2100:
2099:
2098:
2097:
2087:
2083:
2082:
2081:
2080:
2075:
2070:
2059:
2058:
2057:
2052:
2047:
2042:
2031:
2025:
2024:
2023:
2016:
2011:
2006:
2001:
1990:
1989:
1988:
1981:
1976:
1971:
1966:
1955:
1951:
1949:
1947:DNA polymerase
1940:
1931:
1925:
1911:
1910:
1908:
1907:
1902:
1896:
1894:
1889:
1885:
1871:
1870:
1867:
1866:
1864:
1863:
1858:
1853:
1848:
1843:
1838:
1832:
1830:
1825:
1816:
1815:
1813:
1812:
1806:
1804:
1793:
1792:
1790:
1789:
1784:
1778:
1776:
1765:
1764:
1762:
1761:
1756:
1751:
1750:
1749:
1744:
1734:
1732:Diacylglycerol
1729:
1724:
1719:
1714:
1709:
1704:
1699:
1694:
1693:
1692:
1682:
1677:
1672:
1671:
1670:
1665:
1660:
1655:
1650:
1643:Phosphofructo-
1640:
1635:
1634:
1633:
1623:
1618:
1612:
1610:
1596:
1591:
1575:
1574:
1560:
1558:
1557:
1550:
1543:
1535:
1528:
1527:
1498:
1455:
1412:
1369:
1334:
1299:
1271:(8): 2068–76.
1256:
1219:
1188:
1186:
1183:
1180:
1179:
1124:
1075:
1032:
997:
945:
939:10.1101/202820
923:
888:
831:
802:(1): 198–210.
782:
733:
696:Genome Biology
681:
680:
678:
675:
657:
654:
646:anti-microbial
607:
604:
598:and bumps off
549:
535:hydrogen bonds
479:
476:
450:
447:
430:and protein L-
422:Thus, the two
420:
419:
407:
239:
238:
235:
234:
229:
223:
222:
217:
211:
210:
205:
199:
198:
190:
189:
180:
174:
173:
162:
155:
154:
149:
143:
142:
137:
131:
130:
125:
119:
118:
113:
107:
106:
101:
95:
94:
89:
83:
82:
78:
77:
72:
66:
65:
60:
54:
53:
49:
48:
32:
24:
23:
15:
13:
10:
9:
6:
4:
3:
2:
2833:
2822:
2819:
2817:
2814:
2813:
2811:
2801:
2796:
2791:
2787:
2773:
2769:
2768:
2763:
2760:
2756:
2755:
2750:
2747:
2743:
2742:
2737:
2734:
2730:
2729:
2724:
2721:
2717:
2716:
2711:
2708:
2704:
2703:
2698:
2695:
2691:
2690:
2685:
2684:
2682:
2678:
2672:
2669:
2667:
2664:
2662:
2659:
2657:
2654:
2652:
2649:
2648:
2646:
2642:
2636:
2633:
2631:
2630:Enzyme family
2628:
2626:
2623:
2621:
2618:
2617:
2615:
2611:
2605:
2602:
2600:
2597:
2595:
2594:Cooperativity
2592:
2590:
2587:
2586:
2584:
2580:
2574:
2571:
2569:
2566:
2564:
2561:
2559:
2556:
2554:
2553:Oxyanion hole
2551:
2549:
2546:
2544:
2541:
2539:
2536:
2535:
2533:
2529:
2525:
2518:
2513:
2511:
2506:
2504:
2499:
2498:
2495:
2479:
2476:
2474:
2471:
2469:
2466:
2465:
2463:
2460:
2456:
2450:
2449:
2444:
2443:
2441:
2438:
2434:
2428:
2427:
2422:
2421:
2419:
2417:
2413:
2409:
2403:
2402:
2397:
2396:
2394:
2392:
2388:
2384:
2381:
2378:
2370:
2365:
2355:
2352:
2351:
2349:
2345:
2339:
2336:
2334:
2331:
2329:
2326:
2324:
2321:
2320:
2318:
2314:
2311:
2308:
2304:
2294:
2291:
2288:
2284:
2281:
2280:
2278:
2274:
2268:
2265:
2264:
2262:
2260:
2256:
2250:
2247:
2245:
2242:
2241:
2239:
2237:
2233:
2227:
2224:
2222:
2219:
2218:
2216:
2214:
2209:
2205:
2195:
2192:
2190:
2187:
2185:
2182:
2180:
2177:
2173:
2170:
2168:
2165:
2163:
2160:
2159:
2158:
2155:
2151:
2148:
2147:
2146:
2143:
2141:
2138:
2136:
2133:
2131:
2128:
2126:
2123:
2121:
2118:
2116:
2113:
2112:
2110:
2108:
2104:
2096:
2093:
2092:
2091:
2088:
2085:
2084:
2079:
2076:
2074:
2071:
2069:
2066:
2065:
2063:
2060:
2056:
2053:
2051:
2048:
2046:
2043:
2041:
2038:
2037:
2035:
2032:
2029:
2026:
2022:
2021:
2017:
2015:
2012:
2010:
2007:
2005:
2002:
2000:
1997:
1996:
1994:
1991:
1987:
1986:
1982:
1980:
1977:
1975:
1972:
1970:
1967:
1965:
1962:
1961:
1959:
1956:
1953:
1952:
1950:
1948:
1944:
1941:
1939:
1935:
1932:
1929:
1920:
1916:
1912:
1906:
1903:
1901:
1898:
1897:
1895:
1892:
1880:
1876:
1872:
1862:
1859:
1857:
1854:
1852:
1849:
1847:
1844:
1842:
1839:
1837:
1834:
1833:
1831:
1828:
1821:
1817:
1811:
1808:
1807:
1805:
1802:
1798:
1794:
1788:
1785:
1783:
1780:
1779:
1777:
1774:
1770:
1766:
1760:
1757:
1755:
1752:
1748:
1747:Class II PI 3
1745:
1743:
1740:
1739:
1738:
1735:
1733:
1730:
1728:
1725:
1723:
1722:Deoxycytidine
1720:
1718:
1715:
1713:
1710:
1708:
1705:
1703:
1700:
1698:
1695:
1691:
1690:ADP-thymidine
1688:
1687:
1686:
1683:
1681:
1678:
1676:
1673:
1669:
1666:
1664:
1661:
1659:
1656:
1654:
1651:
1649:
1646:
1645:
1644:
1641:
1639:
1636:
1632:
1629:
1628:
1627:
1624:
1622:
1619:
1617:
1614:
1613:
1611:
1608:
1604:
1600:
1597:
1594:
1586:
1582:
1576:
1571:
1567:
1563:
1556:
1551:
1549:
1544:
1542:
1537:
1536:
1533:
1524:
1520:
1516:
1512:
1508:
1504:
1499:
1495:
1491:
1486:
1481:
1477:
1473:
1470:(2): 410–21.
1469:
1465:
1461:
1456:
1452:
1448:
1443:
1438:
1434:
1430:
1426:
1422:
1418:
1413:
1409:
1405:
1401:
1397:
1392:
1387:
1384:(1): 131–41.
1383:
1379:
1375:
1370:
1366:
1362:
1357:
1352:
1348:
1344:
1343:J. Biol. Chem
1340:
1335:
1331:
1327:
1322:
1317:
1313:
1309:
1305:
1300:
1296:
1292:
1287:
1282:
1278:
1274:
1270:
1266:
1262:
1257:
1253:
1249:
1245:
1241:
1237:
1233:
1230:(2): 228–36.
1229:
1225:
1220:
1216:
1212:
1208:
1204:
1200:
1196:
1190:
1189:
1184:
1175:
1171:
1166:
1161:
1156:
1151:
1147:
1143:
1139:
1137:
1128:
1125:
1120:
1116:
1111:
1106:
1102:
1098:
1094:
1090:
1089:Infect. Immun
1086:
1079:
1076:
1071:
1067:
1063:
1059:
1055:
1054:10.1038/86243
1051:
1048:(4): 353–60.
1047:
1043:
1036:
1033:
1028:
1024:
1020:
1016:
1012:
1008:
1001:
998:
993:
989:
984:
979:
975:
971:
967:
963:
959:
952:
950:
946:
940:
935:
927:
924:
919:
915:
911:
907:
903:
899:
892:
889:
884:
880:
875:
870:
866:
862:
858:
854:
850:
846:
842:
835:
832:
827:
823:
818:
813:
809:
805:
801:
797:
793:
786:
783:
778:
774:
769:
764:
760:
756:
752:
748:
744:
737:
734:
729:
725:
720:
715:
710:
705:
701:
697:
693:
686:
683:
676:
674:
672:
668:
663:
655:
653:
651:
647:
643:
639:
638:morphogenesis
635:
631:
627:
623:
622:
617:
613:
605:
603:
601:
597:
593:
589:
583:
581:
576:
571:
567:
558:
546:
542:
540:
536:
532:
528:
523:
521:
516:
512:
511:
506:
502:
497:
493:
489:
485:
477:
475:
472:
464:
460:
455:
448:
446:
443:
441:
437:
433:
429:
425:
397:
396:
395:
394:
390:
386:
382:
378:
374:
373:
368:
364:
360:
356:
352:
349:
345:
340:
337:
333:
329:
325:
321:
317:
313:
312:intracellular
309:
305:
304:growth factor
301:
297:
296:extracellular
293:
289:
285:
281:
277:
274:that exhibit
273:
269:
265:
261:
257:
253:
252:transmembrane
249:
245:
233:
230:
228:
224:
221:
218:
216:
212:
209:
206:
204:
200:
195:
191:
188:
184:
181:
179:
178:Gene Ontology
175:
172:
169:
166:
163:
160:
156:
153:
150:
148:
144:
141:
138:
136:
132:
129:
126:
124:
120:
117:
116:NiceZyme view
114:
112:
108:
105:
102:
100:
96:
93:
90:
88:
84:
79:
76:
73:
71:
67:
64:
61:
59:
55:
50:
44:
40:
35:
30:
25:
20:
2767:Translocases
2764:
2751:
2738:
2725:
2712:
2702:Transferases
2699:
2686:
2543:Binding site
2477:
2445:
2423:
2398:
2019:
1984:
1742:Class I PI 3
1707:Pantothenate
1578:2.7.1-2.7.4:
1562:Transferases
1506:
1503:Biochemistry
1502:
1467:
1464:J. Bacteriol
1463:
1424:
1421:J. Bacteriol
1420:
1381:
1377:
1346:
1342:
1314:(1): 51–61.
1311:
1307:
1268:
1265:J. Bacteriol
1264:
1227:
1223:
1198:
1194:
1145:
1141:
1135:
1127:
1095:(2): 985–7.
1092:
1088:
1078:
1045:
1041:
1035:
1010:
1006:
1000:
965:
961:
926:
901:
897:
891:
848:
844:
834:
799:
795:
785:
750:
746:
736:
699:
695:
685:
670:
666:
661:
659:
633:
619:
609:
588:conformation
584:
563:
527:antiparallel
524:
508:
481:
468:
462:
458:
444:
421:
380:
376:
370:
366:
362:
358:
354:
342:In terms of
341:
247:
243:
242:
104:BRENDA entry
2538:Active site
2293:Transposase
2283:Recombinase
1928:-nucleoside
1754:Sphingosine
650:candidiasis
642:neutrophils
634:C. albicans
626:candidiasis
539:salt bridge
531:hydrophobic
284:phosphatase
260:transferase
92:IntEnz view
75:99283-67-7
52:Identifiers
2810:Categories
2741:Isomerases
2715:Hydrolases
2582:Regulation
2095:Telomerase
1938:Polymerase
1712:Mevalonate
1675:Riboflavin
1566:phosphorus
1013:: 71–112.
677:References
566:nucleotide
496:C-terminal
488:N-terminal
424:substrates
344:enzymology
276:autokinase
272:homodimers
161:structures
128:KEGG entry
2816:EC 2.7.13
2620:EC number
2287:Integrase
2211:3' to 5'
1856:Guanylate
1851:Uridylate
1841:Adenylate
1685:Thymidine
1680:Shikimate
851:: 28–34.
667:S. aureus
632:persons.
449:Mechanism
432:histidine
406:⇌
389:catalyzes
262:class of
81:Databases
2644:Kinetics
2568:Cofactor
2531:Activity
2221:RNase PH
1829:acceptor
1810:Creatine
1803:acceptor
1775:acceptor
1717:Pyruvate
1702:Glycerol
1663:Platelet
1638:Galacto-
1609:acceptor
1523:11705377
1494:17085571
1451:16199567
1408:16842653
1330:15109719
1295:10735847
1252:26038953
1244:14752661
1215:12110368
1174:32354997
1119:11796636
1070:25434861
1062:11276258
992:16319927
918:23863184
883:25844054
826:26140597
777:28129587
753:: 8–16.
728:12372152
501:homology
436:products
383:) is an
351:2.7.13.3
256:proteins
232:proteins
220:articles
208:articles
165:RCSB PDB
63:2.7.13.3
2800:Biology
2754:Ligases
2524:Enzymes
2172:PrimPol
2157:Primase
1631:Hepatic
1626:Fructo-
1485:1797398
1442:1251614
1400:9989504
1365:8132603
1165:7245129
1027:1482126
983:1356327
934:bioRxiv
874:4375673
853:Bibcode
817:4491144
768:5482761
575:adenine
520:β sheet
515:hairpin
492:α helix
484:domains
471:dimeric
300:hormone
264:enzymes
258:of the
187:QuickGO
152:profile
135:MetaCyc
70:CAS no.
2786:Portal
2728:Lyases
2459:2.7.13
2437:2.7.12
2412:2.7.11
2387:2.7.10
2226:PNPase
2194:PNPase
2150:POLRMT
2145:ssRNAP
1658:Muscle
1621:Gluco-
1585:kinase
1521:
1492:
1482:
1449:
1439:
1406:
1398:
1363:
1328:
1293:
1286:111253
1283:
1250:
1242:
1213:
1172:
1162:
1117:
1110:127696
1107:
1068:
1060:
1025:
990:
980:
962:EMBO J
936:
916:
881:
871:
824:
814:
775:
765:
726:
719:244915
716:
580:analog
505:motifs
385:enzyme
316:kinase
282:, and
215:PubMed
197:Search
183:AmiGO
171:PDBsum
111:ExPASy
99:BRENDA
87:IntEnz
58:EC no.
2680:Types
2307:2.7.8
2276:Other
1915:2.7.7
1875:2.7.6
1820:2.7.4
1797:2.7.3
1769:2.7.2
1653:Liver
1616:Hexo-
1603:2.7.1
1404:S2CID
1248:S2CID
1066:S2CID
387:that
381:Sln1p
377:HP165
302:- or
147:PRIAM
2772:list
2765:EC7
2759:list
2752:EC6
2746:list
2739:EC5
2733:list
2726:EC4
2720:list
2713:EC3
2707:list
2700:EC2
2694:list
2687:EC1
2446:see
2424:see
2399:see
1773:COOH
1572:2.7)
1519:PMID
1490:PMID
1447:PMID
1396:PMID
1378:Cell
1361:PMID
1326:PMID
1291:PMID
1240:PMID
1211:PMID
1170:PMID
1115:PMID
1058:PMID
1023:PMID
988:PMID
914:PMID
879:PMID
822:PMID
796:Cell
773:PMID
724:PMID
564:The
463:pros
459:tele
438:are
391:the
355:EnvZ
227:NCBI
168:PDBe
123:KEGG
43:2c2a
2189:PAP
2130:III
2064:/Y
2055:TDT
2036:/X
2028:III
2020:Pfu
1995:/B
1985:Taq
1960:/A
1727:PFP
1697:NAD
1511:doi
1480:PMC
1472:doi
1468:189
1437:PMC
1429:doi
1425:187
1386:doi
1351:doi
1347:269
1316:doi
1312:234
1281:PMC
1273:doi
1269:182
1232:doi
1228:271
1203:doi
1160:PMC
1150:doi
1146:117
1105:PMC
1097:doi
1050:doi
1015:doi
978:PMC
970:doi
906:doi
869:PMC
861:doi
849:367
812:PMC
804:doi
800:162
763:PMC
755:doi
714:PMC
704:doi
671:ica
628:in
600:ADP
570:ATP
440:ADP
428:ATP
372:HK1
332:ATP
203:PMC
159:PDB
39:PDB
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2374:PO
2135:IV
2125:II
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1979:T7
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369:,
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348:EC
278:,
254:,
248:HK
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2009:ε
2004:δ
1999:α
1974:ν
1969:θ
1964:Îł
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