ID ACDB_METTH Reviewed; 460 AA.
AC O27745;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 09-APR-2025, entry version 118.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01138};
DE Short=ACDS complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01138};
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase {ECO:0000255|HAMAP-Rule:MF_01138};
GN Name=cdhC {ECO:0000255|HAMAP-Rule:MF_01138};
GN OrderedLocusNames=MTH_1710;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanobacteria; Methanobacteriales; Methanobacteriaceae;
OC Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon
CC complex generates CO from CO(2), while the beta subunit (this protein)
CC combines the CO with CoA and a methyl group to form acetyl-CoA. The
CC methyl group, which is incorporated into acetyl-CoA, is transferred to
CC the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta
CC complex). {ECO:0000255|HAMAP-Rule:MF_01138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co(I)-[corrinoid Fe-S protein] + acetyl-CoA + H(+) = methyl-
CC Co(III)-[corrinoid Fe-S protein] + CO + CoA; 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:0000255|HAMAP-Rule:MF_01138};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01138};
CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01138}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000255|HAMAP-
CC Rule:MF_01138}.
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DR EMBL; AE000666; AAB86182.1; -; Genomic_DNA.
DR PIR; H69095; H69095.
DR RefSeq; WP_010877318.1; NC_000916.1.
DR AlphaFoldDB; O27745; -.
DR SMR; O27745; -.
DR IntAct; O27745; 1.
DR STRING; 187420.MTH_1710; -.
DR PaxDb; 187420-MTH_1710; -.
DR EnsemblBacteria; AAB86182; AAB86182; MTH_1710.
DR GeneID; 1470795; -.
DR GeneID; 77402228; -.
DR KEGG; mth:MTH_1710; -.
DR PATRIC; fig|187420.15.peg.1671; -.
DR HOGENOM; CLU_613408_0_0_2; -.
DR InParanoid; O27745; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043885; F:anaerobic carbon-monoxide dehydrogenase 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 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; Iron; Iron-sulfur; Metal-binding; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..460
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta"
FT /id="PRO_0000155108"
FT REGION 402..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 191
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 277
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 279
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
SQ SEQUENCE 460 AA; 51737 MW; DB4D50693D154BDA CRC64;
MFEDIPVDVS PMHEGERIRS ANMFVELAGP KSIGAELVQV KDEVEDGKVE VKGPEIDEME
QGQVYPFAIN VEVAGSELEE ELESVIERRL HELCNYVKGF MHLNQRDQIW CRVSTEAKDA
GFRLEHLGKA LSVLFREEFP IIESIAVTLM TDEAAVQEFL ETAREKYETR DSRARELSDE
DVDVFYGCLM CQSFAPTHVC IVTPDRTALC GAINWFDCRA AYKMDPDGPI FEIEKGEVLD
PERGEYANVN AAVEENSQGT TDRVYLHSVF GYPHTSCGCF EAVAFYIPEL DGIGIVNRDF
RGETPLGIPF SAMAGQCSGG KQVEGFSGLS LEYMRSPKFL QADGGYHRVI WMPRELKESV
LEFIPEDVRD KIATEEDATS IKDLRRFLRD NEHPVLERAA VEETEPEEEE VEEAYPEETP
IPEGVPVMAA PEMTLPAAGG FRIVLKNAKI YAEKVIIKRK
//