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Electron-transferring flavoprotein

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203: 37: 406:. ETF consists of three domains: domains I and II are formed by the N- and C-terminal portions of the alpha subunit, respectively, while domain III is formed by the beta subunit. Domains I and III share an almost identical alpha-beta-alpha sandwich fold, while domain II forms an alpha-beta-alpha sandwich similar to that of bacterial 387:. They can be functionally classified into constitutive, "housekeeping" ETFs, mainly involved in the oxidation of fatty acids (Group I), and ETFs produced by some prokaryotes under specific growth conditions, receiving electrons only from the oxidation of specific substrates (Group II). 410:. FAD is bound in a cleft between domains II and III, while domain III binds the AMP molecule. Interactions between domains I and III stabilise the protein, forming a shallow bowl where domain II resides. 474:
Weidenhaupt M, Rossi P, Beck C, Fischer HM, Hennecke H (1996). "Bradyrhizobium japonicum possesses two discrete sets of electron transfer flavoprotein genes: fixA, fixB and etfS, etfL".
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located on the matrix face of the inner mitochondrial membrane and functions as a specific electron acceptor for primary
399: 454: 511:"Phylogenetic characterization of the ubiquitous electron transfer flavoprotein families ETF-alpha and ETF-beta" 439: 429: 418: 335: 169: 403: 331: 165: 449: 288: 122: 624: 583: 532: 491: 322: 156: 573: 563: 522: 483: 314: 148: 552:"Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution" 17: 618: 578: 551: 527: 510: 380: 280: 114: 231: 65: 376: 310: 144: 244: 78: 256: 207:
structure of electron transferring flavoprotein for methylophilus methylotrophus.
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Mutation in ETFs can lead to deficiency of passing reducing equivalent of FADH
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ETFs are heterodimeric proteins composed of an alpha and beta subunit (
268: 263: 102: 97: 383:, transferring the electrons to terminal respiratory systems such as 342: 176: 41:
electron transfer flavoprotein (etf) from paracoccus denitrificans
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Pfam entry for Electron transfer flavoprotein FAD-binding domain
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Pfam entry for Electron transfer flavoprotein domain
341: 321: 303: 298: 274: 262: 250: 237: 225: 217: 212: 195: 175: 155: 137: 132: 108: 96: 84: 71: 59: 51: 46: 29: 196:Electron transfer flavoprotein FAD-binding domain 435:Electron-transferring-flavoprotein dehydrogenase 385:electron-transferring-flavoprotein dehydrogenase 8: 295: 201: 129: 35: 577: 567: 526: 550:Roberts DL, Frerman FE, Kim JJ (1996). 466: 369:electron transfer flavoprotein complex 192: 26: 417:to electron transport chain, causing 30:Electron transfer flavoprotein domain 7: 25: 361:electron transfer flavoprotein 1: 299:Available protein structures: 133:Available protein structures: 556:Proc. Natl. Acad. Sci. U.S.A 528:10.1016/0923-2508(96)80285-3 641: 509:Tsai MH, Saier MH (1995). 455:Oxidative phosphorylation 294: 200: 128: 34: 18:Electron transfer protein 569:10.1073/pnas.93.25.14355 440:Glutaric acidemia type 2 430:Electron transport chain 419:Glutaric acidemia type 2 488:10.1007/s002030050312 450:Microbial metabolism 398:), and contain an 357: 356: 353: 352: 348:structure summary 191: 190: 187: 186: 182:structure summary 16:(Redirected from 632: 592: 591: 581: 571: 562:(25): 14355–60. 547: 541: 540: 530: 506: 500: 499: 471: 296: 205: 193: 130: 39: 27: 21: 640: 639: 635: 634: 633: 631: 630: 629: 615: 614: 601: 596: 595: 549: 548: 544: 508: 507: 503: 476:Arch. Microbiol 473: 472: 468: 463: 426: 416: 208: 42: 23: 22: 15: 12: 11: 5: 638: 636: 628: 627: 617: 616: 613: 612: 607: 600: 599:External links 597: 594: 593: 542: 521:(5): 397–404. 515:Res. Microbiol 501: 465: 464: 462: 459: 458: 457: 452: 447: 442: 437: 432: 425: 422: 414: 381:dehydrogenases 355: 354: 351: 350: 345: 339: 338: 325: 319: 318: 308: 301: 300: 292: 291: 278: 272: 271: 266: 260: 259: 254: 248: 247: 242: 235: 234: 229: 223: 222: 219: 215: 214: 210: 209: 206: 198: 197: 189: 188: 185: 184: 179: 173: 172: 159: 153: 152: 142: 135: 134: 126: 125: 112: 106: 105: 100: 94: 93: 88: 82: 81: 76: 69: 68: 63: 57: 56: 53: 49: 48: 44: 43: 40: 32: 31: 24: 14: 13: 10: 9: 6: 4: 3: 2: 637: 626: 623: 622: 620: 611: 608: 606: 603: 602: 598: 589: 585: 580: 575: 570: 565: 561: 557: 553: 546: 543: 538: 534: 529: 524: 520: 516: 512: 505: 502: 497: 493: 489: 485: 482:(3): 169–78. 481: 477: 470: 467: 460: 456: 453: 451: 448: 446: 443: 441: 438: 436: 433: 431: 428: 427: 423: 421: 420: 411: 409: 405: 402:cofactor and 401: 397: 393: 388: 386: 382: 378: 374: 370: 366: 362: 349: 346: 344: 340: 337: 333: 329: 326: 324: 320: 316: 312: 309: 306: 302: 297: 293: 290: 286: 282: 279: 277: 273: 270: 267: 265: 261: 258: 255: 253: 249: 246: 243: 240: 236: 233: 230: 228: 224: 220: 216: 211: 204: 199: 194: 183: 180: 178: 174: 171: 167: 163: 160: 158: 154: 150: 146: 143: 140: 136: 131: 127: 124: 120: 116: 113: 111: 107: 104: 101: 99: 95: 92: 89: 87: 83: 80: 77: 74: 70: 67: 64: 62: 58: 54: 50: 45: 38: 33: 28: 19: 559: 555: 545: 518: 514: 504: 479: 475: 469: 412: 389: 377:flavoprotein 372: 368: 364: 360: 358: 408:flavodoxins 213:Identifiers 47:Identifiers 461:References 445:Metabolism 311:structures 145:structures 269:PDOC00583 257:IPR014731 221:ETF_alpha 103:PDOC00583 91:IPR014730 625:Proteins 619:Category 424:See also 328:RCSB PDB 252:InterPro 162:RCSB PDB 86:InterPro 588:8962055 537:8525056 496:8599534 375:) is a 264:PROSITE 232:PF00766 98:PROSITE 66:PF01012 586:  576:  535:  494:  343:PDBsum 317:  307:  289:SUPFAM 245:CL0085 218:Symbol 177:PDBsum 151:  141:  123:SUPFAM 79:CL0039 52:Symbol 579:26136 367:) or 285:SCOPe 276:SCOP2 119:SCOPe 110:SCOP2 584:PMID 533:PMID 492:PMID 396:ETFB 394:and 392:ETFA 373:CETF 336:PDBj 332:PDBe 315:ECOD 305:Pfam 281:1efv 241:clan 239:Pfam 227:Pfam 170:PDBj 166:PDBe 149:ECOD 139:Pfam 115:1efv 75:clan 73:Pfam 61:Pfam 574:PMC 564:doi 523:doi 519:146 484:doi 480:165 404:AMP 400:FAD 365:ETF 359:An 323:PDB 157:PDB 55:ETF 621:: 582:. 572:. 560:93 558:. 554:. 531:. 517:. 513:. 490:. 478:. 334:; 330:; 313:/ 287:/ 283:/ 168:; 164:; 147:/ 121:/ 117:/ 590:. 566:: 539:. 525:: 498:. 486:: 415:2 371:( 363:( 20:)

Index

Electron transfer protein

Pfam
PF01012
Pfam
CL0039
InterPro
IPR014730
PROSITE
PDOC00583
SCOP2
1efv
SCOPe
SUPFAM
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary

Pfam
PF00766
Pfam
CL0085
InterPro
IPR014731

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