ID   ACDE2_METTE             Reviewed;         170 AA.
AC   Q9C4Z3;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 71.
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;
OS   Methanosarcina thermophila.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX   PubMed=12464601; DOI=10.1074/jbc.m210484200;
RA   Gencic S., Grahame D.A.;
RT   "Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase
RT   multienzyme complex in methanogens. Catalytic properties and evidence for a
RT   binuclear Ni-Ni site.";
RL   J. Biol. Chem. 278:6101-6110(2003).
RN   [2]
RP   ELECTRON MICROSCOPY OF ALPHA-EPSILON COMPLEX.
RX   PubMed=10600570; DOI=10.1006/jsbi.1999.4163;
RA   Kocsis E., Kessel M., DeMoll E., Grahame D.A.;
RT   "Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA
RT   decarbonylase/synthase complex from Methanosarcina thermophila at 26-A
RT   resolution.";
RL   J. Struct. Biol. 128:165-174(1999).
RN   [3]
RP   CRYSTALLIZATION.
RX   PubMed=12657792; DOI=10.1107/s0907444903001987;
RA   Balbo P., Oliveira M.;
RT   "Crystallization and preliminary X-ray data of the alpha2epsilon2
RT   subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex
RT   from Methanosarcina thermophila.";
RL   Acta Crystallogr. D 59:721-723(2003).
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
CC       (PubMed:10600570, PubMed:12657792). The ACDS complex is made up of
CC       alpha, epsilon, beta, gamma and delta subunits with a probable
CC       stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8)
CC       (By similarity). {ECO:0000255|HAMAP-Rule:MF_01134,
CC       ECO:0000269|PubMed:10600570, ECO:0000269|PubMed:12657792}.
CC   -!- SIMILARITY: Belongs to the CdhB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01134}.
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DR   EMBL; AF173830; AAG53711.1; -; Genomic_DNA.
DR   RefSeq; WP_048168057.1; NZ_CP009502.1.
DR   AlphaFoldDB; Q9C4Z3; -.
DR   SMR; Q9C4Z3; -.
DR   GeneID; 41602249; -.
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   Methanogenesis.
FT   CHAIN           1..170
FT                   /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT                   epsilon 2"
FT                   /id="PRO_0000155096"
SQ   SEQUENCE   170 AA;  18564 MW;  F87CF66E744F427E CRC64;
     MVDTTKNTKL FTSYGVKTSK AITTEVAAKL ISKAKRPLFV VGTGVLDPEL LDRAVKIAKA
     KNIPIAATGS SMPGFVDKDV NAKYINLHQL GFYLTDPDWP GLDGNGNYDT IILLGHKKYY
     INQVLSAVKN FSDVKSISID RNYIQNATMS FGNLSKADHI AALDEVIDLL