ID A0A101W3H6_9FIRM Unreviewed; 726 AA.
AC A0A101W3H6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=CO-methylating acetyl-CoA synthase {ECO:0000256|ARBA:ARBA00012244};
DE EC=2.3.1.169 {ECO:0000256|ARBA:ARBA00012244};
GN ORFNames=APF84_00895 {ECO:0000313|EMBL:KUO65844.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO65844.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO65844.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO65844.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO65844.1}.
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DR EMBL; LOEZ01000019; KUO65844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101W3H6; -.
DR STRING; 1734398.APF84_00895; -.
DR Proteomes; UP000053404; Unassembled WGS sequence.
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 CDD; cd01917; ACS_2; 1.
DR Gene3D; 3.40.50.2030; -; 1.
DR Gene3D; 3.30.1650.10; Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 3; 1.
DR Gene3D; 3.40.1470.10; Bifunctional carbon monoxide dehydrogenase/acetyl-coa synthase(codh/acs), Chain M, domain 5; 1.
DR Gene3D; 3.40.970.20; Carbon monoxide dehydrogenase alpha subunit. Chain D, domain 4; 1.
DR Gene3D; 1.10.8.190; Carbon monoxide dehydrogenase alpha subunit. Chain M, domain 1; 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 NCBIfam; TIGR00316; cdhC; 1.
DR NCBIfam; NF040764; CODH_ACS_al_bet; 1.
DR PANTHER; PTHR42281; -; 1.
DR PANTHER; PTHR42281:SF1; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT BETA 1; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR Pfam; PF18537; CODH_A_N; 1.
DR SUPFAM; SSF56821; Prismane protein-like; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nickel {ECO:0000256|ARBA:ARBA00022596};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 38..119
FT /note="Carbon monoxide dehydrogenase subunit alpha ,N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18537"
FT DOMAIN 482..726
FT /note="CO dehydrogenase/acetyl-CoA synthase complex beta
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19436"
SQ SEQUENCE 726 AA; 81444 MW; 76456864D157E222 CRC64;
MTNFDQIYEG AIEPGKEPRK LFKHAYEGAI TATSYAEILL SKAIKKYGPN QKVEYPDTAY
FLPVIRSLSG EEVKTLKDLQ PILNRMRGKL KSNLNLENVL LAGEATLYAA EIIEALRYVK
NPNPHVEPWT GFLGDPVLRK YGIKMVDWTI PGVAVILGRA KDSKAARKLV DDLMGKGMMI
FLADEIIEQL LEENVKLGID YIAFPVGNFT QVVHAANYAL RAGMAFGGIK PGLREEHRDY
QRRRVLAFVL HLGERDTVKT AAEMGCMFLG FPTITDQVLA EDEQIKDWYV SEPDYDKIVQ
LALEIRGIKL TNIEIDVPIN HGPAFEGETI RKAETYLEMG GGKTPAFEMV RMVEADEIED
GKIEVIGPDI DDISEGDRLP FGLVIDIYGR KMQDDFEGVL ERRVHYFINY GEGLWHVAQR
DLAWLRVSKE AIAKGFKLKH YGELLIAKYK SEFPAIVDRV QVTIYTDQAK VDEMIQVARE
KYAARDARLR GLTDEAVDTF YSCLLCQSFA PNHVCIVTPQ RVGLCGAVSW LDSRASYEIN
PTGPCRPIIK GEAIDEYRGM WKSVNEYVYQ ASNRSLEEVN IYTMMDRPMT SCGCFEAIMA
LVPELNGIMI TTREHSGMTP VGMSFSTLAG MVGGGVQTPG FMGIGRLYLV SKKYIPADGG
IGRILWMPKE LKEFLRDDFV ARSVEEGLGE DFIDKIADET IGVTVEEITP FIEEKGHPAL
TMDPIF
//
