ID   ACDE_METSH              Reviewed;         187 AA.
AC   P26693;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
DE            Short=ACDS CODH subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134};
GN   Name=cdhB {ECO:0000255|HAMAP-Rule:MF_01134};
OS   Methanothrix soehngenii (Methanosaeta concilii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=2223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BLOCKAGE OF N-TERMINUS.
RC   STRAIN=Opfikon / DSM 2139;
RX   PubMed=1901858; DOI=10.1016/s0021-9258(20)89584-2;
RA   Eggen R.I.L., Geerling A.C.M., Jetten M.S.M., de Vos W.M.;
RT   "Cloning, expression, and sequence analysis of the genes for carbon
RT   monoxide dehydrogenase of Methanothrix soehngenii.";
RL   J. Biol. Chem. 266:6883-6887(1991).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC       acetyl-CoA, allowing autotrophic growth from CO(2). The alpha-epsilon
CC       subcomponent functions as a carbon monoxide dehydrogenase. The precise
CC       role of the epsilon subunit is unclear; it may have a stabilizing role
CC       within the alpha(2)epsilon(2) component and/or be involved in electron
CC       transfer to FAD during a potential FAD-mediated CO oxidation.
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; M55280; AAA72935.1; -; Genomic_DNA.
DR   PIR; B39764; B39764.
DR   RefSeq; WP_013719067.1; NC_015416.1.
DR   AlphaFoldDB; P26693; -.
DR   SMR; P26693; -.
DR   GeneID; 10460944; -.
DR   OMA; ITYYYLA; -.
DR   GO; GO:0019385; P:methanogenesis, from acetate; IEA:InterPro.
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;
FT   CHAIN           1..187
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   epsilon"
FT                   /id="PRO_0000155094"
FT   MOD_RES         1
FT                   /note="Blocked amino end (Met)"
SQ   SEQUENCE   187 AA;  21009 MW;  3C8D8FD4F6D8EF18 CRC64;
     MAAEVKKGID TTKNPIPFEM AQIPGPEMAK TYLPKVIGAI IRKAKRPLLV VGAELFDDPV
     MFDKMIEMGK MGIPIAATAH SVKGFVDRGY LENVYQIGLH PLTNFLRFPD WKGLDGQGQY
     DVVIFLGIYY KFANGMLSTL KNFNRDIKRV SIDRYYHVNA DMTFGNLAFN PDDYHAAVDE
     VIAAMKK