ACDE1_METMA
ID ACDE1_METMA Reviewed; 170 AA.
AC Q49162;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit epsilon 1 {ECO:0000255|HAMAP-Rule:MF_01134};
DE Short=ACDS complex subunit epsilon 1 {ECO:0000255|HAMAP-Rule:MF_01134};
DE AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit epsilon 1 {ECO:0000255|HAMAP-Rule:MF_01134};
DE Short=ACDS CODH subunit epsilon 1 {ECO:0000255|HAMAP-Rule:MF_01134};
GN Name=cdhB1; OrderedLocusNames=MM_2088;
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 [GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=8662887; DOI=10.1074/jbc.271.24.14256;
RA Eggen R.I.L., van Kranenburg R., Vriesema A.J.M., Geerling A.C.M.,
RA Verhagen M.F.J.M., Hagen W.R., de Vos W.M.;
RT "Carbon monoxide dehydrogenase from Methanosarcina frisia Go1.
RT Characterization of the enzyme and the regulated expression of two operon-
RT like cdh gene clusters.";
RL J. Biol. Chem. 271:14256-14263(1996).
RN [2]
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 subcomponent functions as a carbon monoxide
CC dehydrogenase. The precise role of the epsilon subunit is unclear; it
CC may have a stabilizing role within the alpha(2)epsilon(2) component
CC and/or be involved in electron transfer to FAD during a potential FAD-
CC mediated CO oxidation. {ECO:0000255|HAMAP-Rule:MF_01134}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8-9.;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000255|HAMAP-Rule:MF_01134}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits. The ACDS
CC complex is made up of alpha, epsilon, beta, gamma and delta subunits
CC with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-
CC (gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01134}.
CC -!- SIMILARITY: Belongs to the CdhB family. {ECO:0000255|HAMAP-
CC Rule:MF_01134}.
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DR EMBL; L26487; AAC37045.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM31784.1; -; Genomic_DNA.
DR RefSeq; WP_011034019.1; NC_003901.1.
DR AlphaFoldDB; Q49162; -.
DR SMR; Q49162; -.
DR STRING; 192952.MM_2088; -.
DR EnsemblBacteria; AAM31784; AAM31784; MM_2088.
DR GeneID; 24840340; -.
DR KEGG; mma:MM_2088; -.
DR PATRIC; fig|192952.21.peg.2397; -.
DR eggNOG; arCOG04408; Archaea.
DR HOGENOM; CLU_123700_0_0_2; -.
DR OMA; ITYYYLA; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01134; CdhB; 1.
DR InterPro; IPR003704; CO_DH_CoA_synth.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR Pfam; PF02552; CO_dh; 1.
DR PIRSF; PIRSF006035; CO_dh_b_ACDS_e; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR TIGRFAMs; TIGR00315; cdhB; 1.
PE 1: Evidence at protein level;
KW Methanogenesis; Reference proteome.
FT CHAIN 1..170
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT epsilon 1"
FT /id="PRO_0000155092"
SQ SEQUENCE 170 AA; 18697 MW; 74B309E6487E3E79 CRC64;
MVDTTKNTKL FTSYGVTTSK AVNPDMVAKM ISKAKRPLFV VGTGVLRPEV LDRAVKIAQK
ANIPIAATGS SLKGFLDKGV DAKYINLHQL GFYLTDPAWP GLDGKGNYDT IIVLEFKKYY
INQVLSGTKN FSNVKAISIG RDYIQNATMS FGNISREDHY AALDELIDNL
