ID ACDB2_METMA Reviewed; 470 AA.
AC Q8PV85;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 127.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2;
DE Short=ACDS complex subunit beta 2;
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase 2;
GN Name=cdhC2; OrderedLocusNames=MM_2087;
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; AAM31783.1; -; Genomic_DNA.
DR RefSeq; WP_011034018.1; NC_003901.1.
DR AlphaFoldDB; Q8PV85; -.
DR SMR; Q8PV85; -.
DR GeneID; 82161143; -.
DR KEGG; mma:MM_2087; -.
DR PATRIC; fig|192952.21.peg.2396; -.
DR eggNOG; arCOG04360; Archaea.
DR HOGENOM; CLU_613408_0_0_2; -.
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; 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; Methanogenesis; Nickel;
KW Transferase.
FT CHAIN 1..470
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 2"
FT /id="PRO_0000155105"
FT BINDING 190
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 279
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 281
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 52364 MW; A6D00D6AA42F7503 CRC64;
MADEFPFEIS PMFEGERVRK EGMFVELGGP KSLGLELVRA ADMDAIEDDK VTIIGPDLKD
MEEGKTYPWA MIFNIGGELV EPDLESVVER RVHDFINYCQ GIMHLNQRYD VWMRVSKDTA
AKMDSFEPFG KAVMMLFKTE LPFIEKMQVT FYTDKDEVEK QMETAKEIFK ARDARTKDLH
DEDVEVFYGC TLCQSFAPTN VCVVSPDRIS LCGAINWFDG RAAAKVDPEG PQFEIAKGDL
IDAVTGEYTG VNEIAKKLSS GEFDKIKLHS FFDCPHTSCG CFEVVGFYIP EVDGIGWVDR
EYQGMAPNGI GFSTMAGQTG GGKQIVGFLG IGVNYFYSPK FIQADGGWNR VVWLPSKLKE
KIDEAIPADL KDKIATENDA SDIESLKAFL QEKNHPVVAT WAAAEEEEEE EEEEEEVAVA
AAPMMMPAAG FQMPAMPMMS GGSSGGIKLT FKNAKITIDR MIISEKKEKK
//
