DCMB_MOOTH
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-AUG-2022, entry version 116.
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; 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.
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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-MON; -.
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 PANTHER; PTHR30109; PTHR30109; 1.
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; 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
