ACDE1_METAC
ID ACDE1_METAC Reviewed; 170 AA.
AC Q8TRZ5;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=MA_1015;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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 -!- 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; AE010299; AAM04445.1; -; Genomic_DNA.
DR RefSeq; WP_011021050.1; NC_003552.1.
DR AlphaFoldDB; Q8TRZ5; -.
DR SMR; Q8TRZ5; -.
DR STRING; 188937.MA_1015; -.
DR PRIDE; Q8TRZ5; -.
DR EnsemblBacteria; AAM04445; AAM04445; MA_1015.
DR GeneID; 1472905; -.
DR KEGG; mac:MA_1015; -.
DR HOGENOM; CLU_123700_0_0_2; -.
DR InParanoid; Q8TRZ5; -.
DR OMA; PYYLSRM; -.
DR OrthoDB; 109783at2157; -.
DR PhylomeDB; Q8TRZ5; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000002487; 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 3: Inferred from homology;
KW Methanogenesis; Reference proteome.
FT CHAIN 1..170
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT epsilon 1"
FT /id="PRO_0000155088"
SQ SEQUENCE 170 AA; 18448 MW; CE7CDD8CE06D87F3 CRC64;
MVDTAKNTKL FTSYGVSTSK TVTPEIAAKL ISKAKRPLLM VGTLTLDPEL LDRVVKISKT
ANIPIAATGS SLASLADKDV DAEYINAHML GFYLTDPNWP GLDGNGNYDT VIVLGFKKFY
INQVLSAAKN FSNLKTIAIE RGYIQNATMS FGNLSKADHY AALDELIDLL