ACDB1_METMA
ID ACDB1_METMA Reviewed; 469 AA.
AC Q8PZ11;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 1;
DE Short=ACDS complex subunit beta 1;
DE EC=2.3.1.169;
DE AltName: Full=ACDS complex acyltransferase 1;
GN Name=cdhC1; OrderedLocusNames=MM_0686;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01138};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Note=Binds 1 [Ni-Fe-S] cluster.;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
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) (Potential).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}.
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DR EMBL; AE008384; AAM30382.1; -; Genomic_DNA.
DR RefSeq; WP_011032637.1; NC_003901.1.
DR AlphaFoldDB; Q8PZ11; -.
DR SMR; Q8PZ11; -.
DR STRING; 192952.MM_0686; -.
DR EnsemblBacteria; AAM30382; AAM30382; MM_0686.
DR GeneID; 24838242; -.
DR KEGG; mma:MM_0686; -.
DR PATRIC; fig|192952.21.peg.817; -.
DR eggNOG; arCOG04360; Archaea.
DR HOGENOM; CLU_613408_0_0_2; -.
DR OMA; YIEGIMH; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000000595; 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; -; 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 PANTHER; PTHR42281; PTHR42281; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR00316; cdhC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..469
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 1"
FT /id="PRO_0000155104"
FT BINDING 189
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 278
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 280
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
SQ SEQUENCE 469 AA; 52233 MW; 804E10AB0B87B6D1 CRC64;
MAEFPFEISP MFEGERVRKE GMFVELGGPK SLGLELVRAA DMDAIEDDKV TIIGPDLKDM
EEGKTYPWAM IFNIGGELVE PDLESVVERR VHDFINYCQG IMHLNQRYDV WMRVSKDTAA
KMDSFEPFGK AVMMLFKTEL PFIEKMQVTF YTDKDEVEKQ METAKEIFKA RDARTKDLHD
EDVEVFYGCT LCQSFAPTNV CVVSPDRISL CGAINWFDGR AAAKVDPEGP QFEIAKGDLL
DAVTGEYTGV NEIAKKLSSG EFDKIKLHSF FDSPHTSCGC FEVVGFYIPE VDGIGWVDRE
YQGMAPNGIG FSTMAGQTGG GKQIVGFLGI GVNYFYSPKF IQADGGWNRV VWLPSKLKEK
IDEAIPADLK DKIATENDAS DIESLKAFLQ EKNHPVVATW AAAEEEEEEE EEEEEVAVAA
APMMMPAAGF QMPAMPMMSG GSSGGIKLTF KNAKITIDRM IISEKKEKK
