DCMA_MOOTH
ID DCMA_MOOTH Reviewed; 729 AA.
AC P27988;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha;
DE Short=ACS subunit;
DE Short=Acetyl-CoA synthase subunit;
DE Short=CODH/ACS;
DE EC=2.3.1.169 {ECO:0000269|PubMed:12386327};
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 PROTEIN SEQUENCE OF 494-508.
RX PubMed=8325380; DOI=10.1016/0014-5793(93)81808-d;
RA Shanmugasundaram T., Sundaresh C.S., Kumar G.K.;
RT "Identification of a cysteine involved in the interaction between carbon
RT monoxide dehydrogenase and corrinoid/Fe-S protein from Clostridium
RT thermoaceticum.";
RL FEBS Lett. 326:281-284(1993).
RN [3]
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 [4]
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 generates CO from CO(2), while the alpha
CC subunit (this protein) 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}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA
CC + methyl-Co(III)-[corrinoid Fe-S protein]; Xref=Rhea:RHEA:45212,
CC Rhea:RHEA-COMP:11110, Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.3.1.169;
CC Evidence={ECO:0000269|PubMed:12386327};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Note=Binds 2 nickel ions per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
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DR EMBL; M62727; AAA23229.1; -; Genomic_DNA.
DR PIR; B41670; B41670.
DR PDB; 1MJG; X-ray; 2.20 A; M/N/O/P=1-729.
DR PDB; 1OAO; X-ray; 1.90 A; C/D=1-729.
DR PDB; 2Z8Y; X-ray; 2.51 A; M/N/O/P=1-729.
DR PDB; 3GIT; X-ray; 3.00 A; A/B/C/D/E/F=311-729.
DR PDB; 3I01; X-ray; 2.15 A; M/N/O/P=1-729.
DR PDB; 3I04; X-ray; 2.15 A; M/N/O/P=2-729.
DR PDB; 3S2X; X-ray; 2.35 A; A/B=594-729.
DR PDB; 5GOL; X-ray; 2.11 A; A/B/C/D=594-728.
DR PDB; 5H6W; X-ray; 2.20 A; A/B/C/D=594-728.
DR PDB; 6X5K; X-ray; 2.47 A; M/N/O/P=1-729.
DR PDBsum; 1MJG; -.
DR PDBsum; 1OAO; -.
DR PDBsum; 2Z8Y; -.
DR PDBsum; 3GIT; -.
DR PDBsum; 3I01; -.
DR PDBsum; 3I04; -.
DR PDBsum; 3S2X; -.
DR PDBsum; 5GOL; -.
DR PDBsum; 5H6W; -.
DR PDBsum; 6X5K; -.
DR AlphaFoldDB; P27988; -.
DR SMR; P27988; -.
DR BioCyc; MetaCyc:CODHALPHACLTH-MON; -.
DR BRENDA; 2.3.1.169; 1528.
DR EvolutionaryTrace; P27988; -.
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:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1650.10; -; 1.
DR Gene3D; 3.40.50.2030; -; 1.
DR InterPro; IPR045822; ACS_CODH_B_C.
DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR InterPro; IPR041350; CODH_A_N.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
DR InterPro; IPR011254; Prismane-like_sf.
DR PANTHER; PTHR42281; PTHR42281; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR Pfam; PF18537; CODH_A_N; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR00316; cdhC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Carbon dioxide fixation; Direct protein sequencing;
KW Iron; Iron-sulfur; Metal-binding; Nickel; Transferase.
FT CHAIN 1..729
FT /note="Carbon monoxide dehydrogenase/acetyl-CoA synthase
FT subunit alpha"
FT /id="PRO_0000079807"
FT BINDING 506
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 509
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 509
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 518
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 528
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT BINDING 595
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 595
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 596
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 596
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT BINDING 597
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT BINDING 597
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 19..47
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 96..117
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 326..330
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:3I01"
FT STRAND 384..391
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 400..412
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 442..455
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:6X5K"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 471..493
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 518..521
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 533..542
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 555..558
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 559..562
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 565..574
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 628..635
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 649..653
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 655..658
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:1OAO"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 672..688
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 695..698
FT /evidence="ECO:0007829|PDB:1OAO"
FT TURN 702..704
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 708..718
FT /evidence="ECO:0007829|PDB:1OAO"
FT HELIX 721..724
FT /evidence="ECO:0007829|PDB:1OAO"
SQ SEQUENCE 729 AA; 81725 MW; 619BB19D959F5A72 CRC64;
MTDFDKIFEG AIPEGKEPVA LFREVYHGAI TATSYAEILL NQAIRTYGPD HPVGYPDTAY
YLPVIRCFSG EEVKKLGDLP PILNRKRAQV SPVLNFENAR LAGEATWYAA EIIEALRYLK
YKPDEPLLPP PWTGFIGDPV VRRFGIKMVD WTIPGEAIIL GRAKDSKALA KIVKELMGMG
FMLFICDEAV EQLLEENVKL GIDYIAYPLG NFTQIVHAAN YALRAGMMFG GVTPGAREEQ
RDYQRRRIRA FVLYLGEHDM VKTAAAFGAI FTGFPVITDQ PLPEDKQIPD WFFSVEDYDK
IVQIAMETRG IKLTKIKLDL PINFGPAFEG ESIRKGDMYV EMGGNRTPAF ELVRTVSESE
ITDGKIEVIG PDIDQIPEGS KLPLGILVDI YGRKMQADFE GVLERRIHDF INYGEGLWHT
GQRNINWLRV SKDAVAKGFR FKNYGEILVA KMKEEFPAIV DRVQVTIFTD EAKVKEYMEV
AREKYKERDD RMRGLTDETV DTFYSCVLCQ SFAPNHVCIV TPERVGLCGA VSWLDAKASY
EINHAGPNQP IPKEGEIDPI KGIWKSVNDY LYTASNRNLE QVCLYTLMEN PMTSCGCFEA
IMAILPECNG IMITTRDHAG MTPSGMTFST LAGMIGGGTQ TPGFMGIGRT YIVSKKFISA
DGGIARIVWM PKSLKDFLHD EFVRRSVEEG LGEDFIDKIA DETIGTTVDE ILPYLEEKGH
PALTMDPIM
