ID D5EBX2_METMS Unreviewed; 465 AA.
AC D5EBX2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01138};
DE Short=ACDS complex subunit beta {ECO:0000256|HAMAP-Rule:MF_01138};
DE EC=2.3.1.169 {ECO:0000256|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase {ECO:0000256|HAMAP-Rule:MF_01138};
GN Name=cdhC {ECO:0000256|HAMAP-Rule:MF_01138};
GN OrderedLocusNames=Mmah_1168 {ECO:0000313|EMBL:ADE36673.1};
OS Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36673.1, ECO:0000313|Proteomes:UP000001059};
RN [1] {ECO:0000313|EMBL:ADE36673.1, ECO:0000313|Proteomes:UP000001059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35705 / DSM 5219 / SLP
RC {ECO:0000313|Proteomes:UP000001059};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Methanohalophilus mahii DSM 5219.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC acetyl-CoA, allowing growth on acetate as sole source of carbon and
CC energy. The alpha-epsilon complex generates CO from CO(2), while the
CC beta subunit (this protein) combines the CO with CoA and a methyl group
CC to form acetyl-CoA. The methyl group, which is incorporated into
CC acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-
CC sulfur protein (the gamma-delta complex). {ECO:0000256|HAMAP-
CC Rule:MF_01138}.
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:0000256|HAMAP-Rule:MF_01138};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01138};
CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000256|HAMAP-Rule:MF_01138};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000256|ARBA:ARBA00004905, ECO:0000256|HAMAP-Rule:MF_01138}.
CC -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, beta,
CC gamma and delta chains with a probable stoichiometry of
CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
CC {ECO:0000256|ARBA:ARBA00025865, ECO:0000256|HAMAP-Rule:MF_01138}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000256|ARBA:ARBA00006862,
CC ECO:0000256|HAMAP-Rule:MF_01138}.
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DR EMBL; CP001994; ADE36673.1; -; Genomic_DNA.
DR RefSeq; WP_013037615.1; NC_014002.1.
DR AlphaFoldDB; D5EBX2; -.
DR STRING; 547558.Mmah_1168; -.
DR GeneID; 8983335; -.
DR KEGG; mmh:Mmah_1168; -.
DR HOGENOM; CLU_613408_0_0_2; -.
DR OrthoDB; 69951at2157; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000001059; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01138; CdhC; 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; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc.
DR InterPro; IPR011254; Prismane-like_sf.
DR NCBIfam; TIGR00316; cdhC; 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 SUPFAM; SSF56821; Prismane protein-like; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_01138}; Coiled coil {ECO:0000256|SAM:Coils};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01138};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01138};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01138}; Methanogenesis {ECO:0000256|HAMAP-Rule:MF_01138};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|HAMAP-Rule:MF_01138};
KW Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01138}.
FT DOMAIN 170..399
FT /note="CO dehydrogenase/acetyl-CoA synthase complex beta
FT subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19436"
FT REGION 401..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 145..176
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 191
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01138"
FT BINDING 194
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01138"
FT BINDING 280
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01138"
FT BINDING 282
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01138"
SQ SEQUENCE 465 AA; 52242 MW; 3F539926FC6EFB9B CRC64;
MAEDFPFEIS PMFEGERIRK NDMYVELSGP KSIGFELVKA AEMDDVVDGK FNMIGPDVQD
MEEGGRYPFA MIYKIAGELV EEDLESIVER RNHDFQNYIQ GLMHLNQRYD VWVRLSKEAV
EKGVTSFESI AQAIMMLFKN ELPFIEKVEA TYITDKDEIE KLMDEAKAKY KARDDRTRNL
HDEDVDTFYG CTLCQSFAPS NVCVITPDRI SLCGAINWFD GRAAAKVDPE GPQFAIPKGD
VIDDESGEYT GVNETAKSLS SGEYDRIKLH SFFDYPHTSC GCFEVVGFYI PEVDGIGWVD
RDFTGAAPNG LPFSTMAGQT GGGKQISGFL GIGINYFRSP KFIQSDGGWE RVVWMPKHLK
DRVADDIPDD IADKIATEED VSDLETLRNF LKEKKHPIVN RWEKEEEEEA AEEEETPQQT
APAMQMPASM PMNMPAMPSS GSGGVKVILK NAKVSVDKII IKNNE
//
