ID   ACDE1_ARCFU             Reviewed;         184 AA.
AC   O29164;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=AF_1101;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90135.1; -; Genomic_DNA.
DR   PIR; D69387; D69387.
DR   AlphaFoldDB; O29164; -.
DR   SMR; O29164; -.
DR   STRING; 224325.AF_1101; -.
DR   EnsemblBacteria; AAB90135; AAB90135; AF_1101.
DR   KEGG; afu:AF_1101; -.
DR   eggNOG; arCOG04408; Archaea.
DR   HOGENOM; CLU_123700_0_0_2; -.
DR   OMA; PYYLSRM; -.
DR   PhylomeDB; O29164; -.
DR   BioCyc; MetaCyc:AF_RS05565-MON; -.
DR   Proteomes; UP000002199; Chromosome.
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   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..184
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   epsilon 1"
FT                   /id="PRO_0000155086"
SQ   SEQUENCE   184 AA;  20908 MW;  100E15863EA2807E CRC64;
     MMEMAVAKEE KFPTAKRFDI ADIQVSREAT AVKPKVVANM IKRAKRPLLV TGGQLLKDEK
     LVEFAVKFAE KGIPIAATAG SSKPLIERGI KPVSKTYTLH QITQFLQDEE FQGFDGNGNY
     DTVIFLGFLP YYLSRMLSSL KHFSKITTIA IDEFYQPHAK FSFTNLTKDR ELYYSMLQEV
     LDNL