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 13-SEP-2023, entry version 120. 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; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella. OX NCBI_TaxID=1525; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1748656; DOI=10.1016/s0021-9258(18)54357-x; RA Morton T.A., Runquist J.A., Ragsdale S.W., Shanmugasundaram T., Wood H.G., RA 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, AND RP 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 dehydrogenase/acetyl- RT 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., Lindahl P.A., RA Fontecilla-Camps J.-C.; RT "Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of RT 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 group to CC form acetyl-CoA. The methyl group, which is incorporated into acetyl- CC CoA, is transferred to the alpha subunit by a corrinoid iron-sulfur CC protein. {ECO:0000269|PubMed:12386327, ECO:0000269|PubMed:12627225}. CC -!- CATALYTIC ACTIVITY: CC Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2 H(+) + 2 CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4; CC Evidence={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 RefSeq; WP_011392717.1; NZ_VCDY01000001.1. 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 PDB; 6X5K; X-ray; 2.47 A; A/B/C/D=1-674. DR PDBsum; 1MJG; -. DR PDBsum; 1OAO; -. DR PDBsum; 2Z8Y; -. DR PDBsum; 3I01; -. DR PDBsum; 3I04; -. DR PDBsum; 6X5K; -. DR AlphaFoldDB; P27989; -. DR SMR; P27989; -. DR OMA; LMAGCNN; -. DR BioCyc; MetaCyc:CODHBETACLTH-MONOMER; -. DR BRENDA; 1.2.7.4; 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:UniProtKB-EC. 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 CDD; cd01915; CODH; 1. 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; IPR016099; Prismane-like_a/b-sand. DR InterPro; IPR011254; Prismane-like_sf. DR NCBIfam; TIGR01702; CO_DH_cata; 1. DR PANTHER; PTHR30109:SF4; CARBON MONOXIDE DEHYDROGENASE; 1. DR PANTHER; PTHR30109; HYDROXYLAMINE REDUCTASE; 1. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR SUPFAM; SSF56821; Prismane protein-like; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Carbon dioxide fixation; Electron transport; Iron; KW Iron-sulfur; Metal-binding; Nickel; Oxidoreductase; Transport. FT CHAIN 1..674 FT /note="Carbon monoxide dehydrogenase/acetyl-CoA synthase FT subunit beta" FT /id="PRO_0000079808" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 59 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 68 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 71 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 76 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 90 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT BINDING 283 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT BINDING 317 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT BINDING 355 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT BINDING 470 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT BINDING 500 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT BINDING 550 FT /ligand="[Ni-4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:47739" FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 31..43 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 48..55 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 81..83 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 94..128 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 140..149 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 159..175 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 192..200 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 208..218 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 227..256 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 262..267 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 275..283 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 285..297 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 299..304 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 310..315 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 316..326 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 330..332 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 334..336 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 337..341 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 347..351 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 353..355 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 360..364 FT /evidence="ECO:0007829|PDB:1OAO" FT TURN 365..368 FT /evidence="ECO:0007829|PDB:3I01" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 390..392 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 393..412 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 425..429 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 433..441 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 449..457 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 463..467 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 479..490 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 493..498 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 499..507 FT /evidence="ECO:0007829|PDB:1OAO" FT TURN 508..511 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 513..515 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 516..519 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 522..534 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 543..549 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 553..567 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 571..573 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 576..580 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 586..597 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 601..606 FT /evidence="ECO:0007829|PDB:1OAO" FT TURN 609..612 FT /evidence="ECO:0007829|PDB:3I01" FT HELIX 614..621 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 623..627 FT /evidence="ECO:0007829|PDB:1OAO" FT STRAND 631..634 FT /evidence="ECO:0007829|PDB:1OAO" FT HELIX 638..666 FT /evidence="ECO:0007829|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 //