ID   ACDE2_METAC             Reviewed;         170 AA.
AC   Q8TJC5;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit epsilon 2 {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS complex subunit epsilon 2 {ECO:0000255|HAMAP-Rule:MF_01134};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit epsilon 2 {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS CODH subunit epsilon 2 {ECO:0000255|HAMAP-Rule:MF_01134};
GN   Name=cdhB2; OrderedLocusNames=MA_3861;
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; AAM07212.1; -; Genomic_DNA.
DR   RefSeq; WP_011023759.1; NC_003552.1.
DR   AlphaFoldDB; Q8TJC5; -.
DR   SMR; Q8TJC5; -.
DR   STRING; 188937.MA_3861; -.
DR   EnsemblBacteria; AAM07212; AAM07212; MA_3861.
DR   GeneID; 1475754; -.
DR   KEGG; mac:MA_3861; -.
DR   HOGENOM; CLU_123700_0_0_2; -.
DR   InParanoid; Q8TJC5; -.
DR   OMA; ITYYYLA; -.
DR   OrthoDB; 109783at2157; -.
DR   PhylomeDB; Q8TJC5; -.
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 2"
FT                   /id="PRO_0000155089"
SQ   SEQUENCE   170 AA;  18466 MW;  25B146E225041208 CRC64;
     MVDTTKNTKL FTSYGVTTSK TTTPEIAAKL ISKAKRPLLV VGTKVLDPEL LDRAVKIAQK
     ANIPIAATGS SMPGFVGKDV DAKYINLHQL GFYVTDPNWP GLDGNGTYDT LIVLGHIKYY
     INQVLSGTKN FSTVKAIAIE RNYIQNATMS FGNLSKADHY AALDELIDAL