ACDE1_METTE
ID ACDE1_METTE Reviewed; 170 AA.
AC P72020;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 77.
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;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8955306; DOI=10.1128/jb.178.23.6849-6856.1996;
RA Maupin-Furlow J.A., Ferry J.G.;
RT "Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of
RT Methanosarcina thermophila.";
RL J. Bacteriol. 178:6849-6856(1996).
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 -!- 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; U66032; AAC44651.1; -; Genomic_DNA.
DR AlphaFoldDB; P72020; -.
DR SMR; P72020; -.
DR KEGG; ag:AAC44651; -.
DR BioCyc; MetaCyc:CDHBMSARC-MON; -.
DR UniPathway; UPA00642; -.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IDA:MENGO.
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 Direct protein sequencing; Methanogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8955306"
FT CHAIN 2..170
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT epsilon 1"
FT /id="PRO_0000155095"
SQ SEQUENCE 170 AA; 18740 MW; 5534CA08ACF51663 CRC64;
MVDTTKNTKL FTSYGVTTSK AINPDMAAKM ISKAKRPLFV VGTGVLRPEI LDRAVKIAKK
ANLPIAATGS SLNGFLDKDV DAKYINVHQL GFYLTDPAWP GLDGKGNYDT IIILEFKKYY
INQVLSGTKN FSKVKSISIG KDYIQNATMS FGNISREEHF AALDELIDLL