ID DCMB_MOOTH Reviewed; 674 AA. AC P27989; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 02-NOV-2016, entry version 99. DE RecName: Full=Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta; DE Short=CODH subunit; DE Short=CODH/ACS; DE Short=Carbon monoxide dehydrogenase subunit; DE EC=1.2.7.4; OS Moorella thermoacetica (Clostridium thermoaceticum). OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Moorella group; Moorella. OX NCBI_TaxID=1525; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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), FUNCTION, CATALYTIC ACTIVITY, RP AND REACTION MECHANISM. 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), AND REACTION MECHANISM. 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. {ECO:0000269|PubMed:12386327, CC ECO:0000269|PubMed:12627225}. CC -!- CATALYTIC ACTIVITY: CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 CC reduced ferredoxin + 2 H(+). {ECO:0000269|PubMed:12627225}. CC -!- COFACTOR: CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; CC Note=Binds 1 [Ni-Fe-S] cluster per subunit.; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=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; 2.20 A; A/B/C/D=1-674. DR PDB; 1OAO; X-ray; 1.90 A; A/B=1-674. DR PDB; 2Z8Y; X-ray; 2.51 A; A/B/C/D=1-674. DR PDB; 3I01; X-ray; 2.15 A; A/B/C/D=1-674. DR PDB; 3I04; X-ray; 2.15 A; A/B/C/D=2-674. DR PDBsum; 1MJG; -. DR PDBsum; 1OAO; -. DR PDBsum; 2Z8Y; -. DR PDBsum; 3I01; -. DR PDBsum; 3I04; -. DR ProteinModelPortal; P27989; -. DR SMR; P27989; -. DR STRING; 264732.Moth_1203; -. DR eggNOG; ENOG4105CJG; Bacteria. DR eggNOG; COG1151; LUCA. DR BioCyc; MetaCyc:CODHBETACLTH-MONOMER; -. DR BRENDA; 1.2.99.2; 1528. DR BRENDA; 2.3.1.169; 1528. DR EvolutionaryTrace; P27989; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro. DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro. DR Gene3D; 1.20.1270.30; -; 1. DR Gene3D; 3.40.50.2030; -; 2. DR InterPro; IPR016101; CO_DH_a-bundle. DR InterPro; IPR010047; CODH. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR01702; CO_DH_cata; 1. PE 1: Evidence at protein level; 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 subunit beta. 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); via tele FT nitrogen. 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 18 21 {ECO:0000244|PDB:1OAO}. FT HELIX 31 43 {ECO:0000244|PDB:1OAO}. FT HELIX 48 55 {ECO:0000244|PDB:1OAO}. FT HELIX 60 63 {ECO:0000244|PDB:1OAO}. FT STRAND 81 83 {ECO:0000244|PDB:1OAO}. FT HELIX 94 128 {ECO:0000244|PDB:1OAO}. FT HELIX 140 149 {ECO:0000244|PDB:1OAO}. FT HELIX 159 175 {ECO:0000244|PDB:1OAO}. FT HELIX 184 187 {ECO:0000244|PDB:1OAO}. FT HELIX 192 200 {ECO:0000244|PDB:1OAO}. FT HELIX 208 218 {ECO:0000244|PDB:1OAO}. FT HELIX 227 256 {ECO:0000244|PDB:1OAO}. FT STRAND 262 267 {ECO:0000244|PDB:1OAO}. FT HELIX 268 270 {ECO:0000244|PDB:1OAO}. FT STRAND 275 283 {ECO:0000244|PDB:1OAO}. FT HELIX 285 297 {ECO:0000244|PDB:1OAO}. FT HELIX 299 304 {ECO:0000244|PDB:1OAO}. FT STRAND 310 315 {ECO:0000244|PDB:1OAO}. FT HELIX 316 326 {ECO:0000244|PDB:1OAO}. FT STRAND 330 332 {ECO:0000244|PDB:1OAO}. FT HELIX 334 336 {ECO:0000244|PDB:1OAO}. FT HELIX 337 341 {ECO:0000244|PDB:1OAO}. FT STRAND 347 351 {ECO:0000244|PDB:1OAO}. FT STRAND 353 355 {ECO:0000244|PDB:1OAO}. FT HELIX 360 364 {ECO:0000244|PDB:1OAO}. FT TURN 365 368 {ECO:0000244|PDB:3I01}. FT STRAND 370 373 {ECO:0000244|PDB:1OAO}. FT STRAND 383 385 {ECO:0000244|PDB:1OAO}. FT HELIX 390 392 {ECO:0000244|PDB:1OAO}. FT HELIX 393 412 {ECO:0000244|PDB:1OAO}. FT STRAND 414 416 {ECO:0000244|PDB:1OAO}. FT STRAND 425 429 {ECO:0000244|PDB:1OAO}. FT HELIX 433 441 {ECO:0000244|PDB:1OAO}. FT HELIX 449 457 {ECO:0000244|PDB:1OAO}. FT STRAND 463 467 {ECO:0000244|PDB:1OAO}. FT HELIX 479 490 {ECO:0000244|PDB:1OAO}. FT STRAND 493 498 {ECO:0000244|PDB:1OAO}. FT HELIX 499 507 {ECO:0000244|PDB:1OAO}. FT TURN 508 511 {ECO:0000244|PDB:1OAO}. FT HELIX 513 515 {ECO:0000244|PDB:1OAO}. FT HELIX 516 519 {ECO:0000244|PDB:1OAO}. FT HELIX 522 534 {ECO:0000244|PDB:1OAO}. FT STRAND 543 549 {ECO:0000244|PDB:1OAO}. FT HELIX 550 552 {ECO:0000244|PDB:1OAO}. FT HELIX 553 567 {ECO:0000244|PDB:1OAO}. FT HELIX 571 573 {ECO:0000244|PDB:1OAO}. FT STRAND 576 580 {ECO:0000244|PDB:1OAO}. FT HELIX 586 597 {ECO:0000244|PDB:1OAO}. FT STRAND 601 606 {ECO:0000244|PDB:1OAO}. FT TURN 609 612 {ECO:0000244|PDB:3I01}. FT HELIX 614 621 {ECO:0000244|PDB:1OAO}. FT HELIX 623 627 {ECO:0000244|PDB:1OAO}. FT STRAND 631 634 {ECO:0000244|PDB:1OAO}. FT HELIX 638 666 {ECO:0000244|PDB:1OAO}. 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 //