ID DCMB_MOOTH STANDARD; PRT; 674 AA. AC P27989; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 07-FEB-2006, entry version 44. DE Carbon monoxide dehydrogenase/acetyl CoA synthase beta subunit DE (EC 1.2.7.4) (EC 1.2.99.2) (Carbon monoxide dehydrogenase subunit) DE (CODH/ACS) (CODH subunit). OS Moorella thermoacetica (Clostridium thermoaceticum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacteriales; OC Thermoanaerobacteriaceae; Moorella group; Moorella. OX NCBI_TaxID=1525; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92084676; PubMed=1748656; RA Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., RA Wood H.G., Ljungdahl L.G.; RT "The primary structure of the subunits of carbon monoxide RT dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum."; RL J. Biol. Chem. 266:23824-23828(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=12386327; DOI=10.1126/science.1075843; RA Doukov T.I., Iverson T.M., Seravalli J., Ragsdale S.W., Drennan C.L.; RT "A Ni-Fe-Cu center in a bifunctional carbon monoxide RT dehydrogenase/acetyl-CoA synthase."; RL Science 298:567-572(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=12627225; DOI=10.1038/nsb912; RA Darnault C., Volbeda A., Kim E.J., Legrand P., Vernede X., RA Lindahl P.A., Fontecilla-Camps J.-C.; RT "Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open RT subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase."; RL Nat. Struct. Biol. 10:271-279(2003). CC -!- FUNCTION: The beta subunit (this protein) generates CO from CO(2), CC while the alpha subunit combines the CO with CoA and a methyl CC group to form acetyl-CoA. The methyl group, which is incorporated CC into acetyl-CoA, is transferred to the alpha subunit by a CC corrinoid iron-sulfur protein. CC -!- CATALYTIC ACTIVITY: CO + H(2)O + oxidized ferredoxin = CO(2) + CC reduced ferredoxin. CC -!- CATALYTIC ACTIVITY: CO + H(2)O + A = CO(2) + AH(2). CC -!- COFACTOR: Binds 1 Nickel-iron-sulfur cluster per subunit. CC -!- COFACTOR: Binds 2 4Fe-4S clusters per homodimer. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M62727; AAA23228.1; -; Genomic_DNA. DR PIR; A41670; A41670. DR PDB; 1MJG; X-ray; A/B/C/D=1-674. DR PDB; 1OAO; X-ray; A/B=1-674. DR InterPro; IPR002110; ANK. DR InterPro; IPR010047; CODH_cata. DR InterPro; IPR004137; Prismane. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR PRINTS; PR01415; ANKYRIN. DR TIGRFAMs; TIGR01702; CO_DH_cata; 1. KW 3D-structure; 4Fe-4S; Carbon dioxide fixation; Electron transport; KW Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase; Transport. FT CHAIN 1 674 Carbon monoxide dehydrogenase/acetyl CoA FT synthase beta subunit. FT /FTId=PRO_0000079808. FT METAL 59 59 Iron-sulfur 1 (4Fe-4S) (shared with FT dimeric partner). FT METAL 67 67 Iron-sulfur 1 (4Fe-4S) (shared with FT dimeric partner). FT METAL 68 68 Iron-sulfur 2 (4Fe-4S). FT METAL 71 71 Iron-sulfur 2 (4Fe-4S). FT METAL 76 76 Iron-sulfur 2 (4Fe-4S). FT METAL 90 90 Iron-sulfur 2 (4Fe-4S). FT METAL 283 283 Nickel-iron-sulfur (Ni-4Fe-4S). FT METAL 317 317 Nickel-iron-sulfur (Ni-4Fe-4S). FT METAL 355 355 Nickel-iron-sulfur (Ni-4Fe-4S). FT METAL 470 470 Nickel-iron-sulfur (Ni-4Fe-4S). FT METAL 500 500 Nickel-iron-sulfur (Ni-4Fe-4S). FT METAL 550 550 Nickel-iron-sulfur (Ni-4Fe-4S). FT STRAND 5 6 FT TURN 7 8 FT STRAND 11 12 FT STRAND 15 15 FT STRAND 18 21 FT TURN 22 23 FT STRAND 25 25 FT STRAND 28 28 FT HELIX 31 43 FT TURN 44 44 FT HELIX 48 55 FT STRAND 57 57 FT HELIX 60 63 FT TURN 64 65 FT STRAND 67 68 FT STRAND 70 71 FT TURN 72 73 FT STRAND 76 77 FT STRAND 81 83 FT TURN 84 85 FT STRAND 86 87 FT TURN 89 90 FT STRAND 93 93 FT HELIX 94 128 FT TURN 129 130 FT STRAND 131 131 FT TURN 133 134 FT STRAND 138 138 FT HELIX 140 149 FT TURN 150 151 FT TURN 155 156 FT HELIX 159 175 FT TURN 178 179 FT STRAND 180 180 FT HELIX 184 187 FT TURN 188 189 FT STRAND 190 190 FT HELIX 192 200 FT TURN 201 202 FT STRAND 206 207 FT HELIX 208 218 FT TURN 219 219 FT STRAND 220 220 FT TURN 221 222 FT STRAND 223 223 FT HELIX 227 256 FT STRAND 262 267 FT HELIX 268 270 FT TURN 273 274 FT STRAND 275 283 FT HELIX 285 297 FT TURN 298 298 FT HELIX 299 304 FT TURN 305 306 FT STRAND 308 308 FT STRAND 310 315 FT HELIX 316 326 FT STRAND 330 332 FT HELIX 334 341 FT TURN 342 343 FT STRAND 344 344 FT STRAND 347 351 FT STRAND 353 355 FT TURN 358 359 FT HELIX 360 364 FT TURN 365 366 FT STRAND 367 368 FT STRAND 370 373 FT STRAND 375 375 FT TURN 376 377 FT STRAND 378 378 FT TURN 381 382 FT STRAND 383 385 FT HELIX 390 412 FT TURN 413 413 FT STRAND 414 416 FT STRAND 425 429 FT HELIX 433 441 FT TURN 442 443 FT STRAND 445 446 FT TURN 448 448 FT HELIX 449 457 FT TURN 458 459 FT STRAND 460 461 FT STRAND 463 467 FT TURN 473 474 FT STRAND 475 475 FT STRAND 477 477 FT TURN 478 478 FT HELIX 479 490 FT TURN 491 492 FT STRAND 493 498 FT HELIX 499 507 FT TURN 508 511 FT HELIX 513 519 FT HELIX 522 534 FT TURN 535 536 FT STRAND 538 539 FT STRAND 543 549 FT HELIX 550 567 FT TURN 568 568 FT STRAND 569 569 FT HELIX 571 573 FT STRAND 574 574 FT STRAND 576 580 FT TURN 581 582 FT STRAND 585 585 FT HELIX 586 597 FT TURN 598 599 FT STRAND 601 606 FT STRAND 609 609 FT TURN 611 612 FT HELIX 614 621 FT TURN 622 622 FT HELIX 623 627 FT TURN 628 628 FT STRAND 629 629 FT STRAND 631 634 FT STRAND 636 637 FT HELIX 638 666 FT TURN 667 667 SQ SEQUENCE 674 AA; 72924 MW; 54BA3D816C25F9FC CRC64; MPRFRDLSHN CRPSEAPRVM EPKNRDRTVD PAVLEMLVKS KDDKVITAFD RFVAQQPQCK IGYEGICCRF CMAGPCRIKA TDGPGSRGIC GASAWTIVAR NVGLMILTGA AAHCEHGNHI AHALVEMAEG KAPDYSVKDE AKLKEVCRRV GIEVEGKSVL ELAQEVGEKA LEDFRRLKGE GEATWLMTTI NEGRKEKFRT HNVVPFGIHA SISELVNQAH MGMDNDPVNL VFSAIRVALA DYTGEHIATD FSDILFGTPQ PVVSEANMGV LDPDQVNFVL HGHNPLLSEI IVQAAREMEG EAKAAGAKGI NLVGICCTGN EVLMRQGIPL VTSFASQELA ICTGAIDAMC VDVQCIMPSI SAVAECYHTR IITTADNAKI PGAYHIDYQT ATAIESAKTA IRMAIEAFKE RKESNRPVYI PQIKNRVVAG WSLEALTKLL ATQNAQNPIR VLNQAILDGE LAGVALICGC NNLKGFQDNS HLTVMKELLK NNVFVVATGC SAQAAGKLGL LDPANVETYC GDGLKGFLKR LGEGANIEIG LPPVFHMGSC VDNSRAVDLL MAMANDLGVD TPKVPFVASA PEAMSGKAAA IGTWWVSLGV PTHVGTMPPV EGSDLIYSIL TQIASDVYGG YFIFEMDPQV AARKILDALE YRTWKLGVHK EVAERYETKL CQGY //