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 03-MAR-2009, entry version 67. DE RecName: Full=Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit beta; DE Short=CODH/ACS; DE Short=Carbon monoxide dehydrogenase subunit; DE Short=CODH subunit; DE EC=1.2.7.4; DE EC=1.2.99.2; 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 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 + 2 oxidized ferredoxin = CO(2) + 2 CC reduced ferredoxin + 2 H(+). 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; 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 PDBsum; 1MJG; -. DR PDBsum; 1OAO; -. DR PDBsum; 2Z8Y; -. DR BRENDA; 1.2.7.4; 14822. DR BRENDA; 1.2.99.2; 14822. DR LinkHub; P27989; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) ac...; IEA:InterPro. DR GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) ...; IEA:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel ion binding; IEA:InterPro. DR GO; GO:0015977; P:carbon utilization by fixation of carbon di...; IEA:UniProtKB-KW. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR016101; CO_DHase_a-bundle. DR InterPro; IPR010047; CO_DHase_cat. DR InterPro; IPR004137; Prismane. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR Gene3D; G3DSA:1.20.1270.30; CO_DH_a-bundle; 1. DR Gene3D; G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 2. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR PRINTS; PR01415; ANKYRIN. 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 FT HELIX 31 42 FT HELIX 48 55 FT HELIX 60 63 FT STRAND 81 83 FT HELIX 94 128 FT HELIX 140 149 FT HELIX 159 175 FT HELIX 184 187 FT HELIX 192 200 FT HELIX 208 219 FT HELIX 227 256 FT STRAND 262 267 FT HELIX 268 270 FT STRAND 275 283 FT HELIX 285 296 FT HELIX 299 304 FT STRAND 310 315 FT HELIX 316 326 FT STRAND 330 332 FT HELIX 334 336 FT HELIX 337 341 FT STRAND 348 351 FT STRAND 353 355 FT HELIX 360 364 FT TURN 365 368 FT STRAND 370 373 FT STRAND 383 385 FT HELIX 390 392 FT HELIX 393 412 FT STRAND 425 429 FT HELIX 433 441 FT HELIX 448 457 FT STRAND 463 467 FT HELIX 479 490 FT STRAND 493 498 FT HELIX 499 507 FT TURN 508 511 FT HELIX 513 515 FT HELIX 516 519 FT HELIX 522 534 FT STRAND 543 550 FT HELIX 553 567 FT HELIX 571 573 FT STRAND 574 580 FT HELIX 586 597 FT STRAND 601 606 FT TURN 609 612 FT HELIX 614 621 FT HELIX 623 627 FT STRAND 631 634 FT HELIX 638 665 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 //