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   27-MAR-2024, entry version 115.
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; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; 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=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: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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 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: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   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..417
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
//