ACDE2_ARCFU
ID ACDE2_ARCFU Reviewed; 175 AA.
AC O30273;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 115.
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=AF_2398;
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).
RN [2]
RP PROTEIN SEQUENCE OF 2-30.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9575239; DOI=10.1007/s002030050606;
RA Dai Y.R., Reed D.W., Millstein J.H., Hartzell P.L., Grahame D.A.,
RA DeMoll E.;
RT "Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.";
RL Arch. Microbiol. 169:525-529(1998).
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; AAB91265.1; -; Genomic_DNA.
DR PIR; G69549; G69549.
DR RefSeq; WP_010879885.1; NC_000917.1.
DR PDB; 1YTL; X-ray; 1.80 A; A/B/C/D=2-175.
DR PDBsum; 1YTL; -.
DR AlphaFoldDB; O30273; -.
DR SMR; O30273; -.
DR STRING; 224325.AF_2398; -.
DR EnsemblBacteria; AAB91265; AAB91265; AF_2398.
DR GeneID; 1485628; -.
DR KEGG; afu:AF_2398; -.
DR eggNOG; arCOG04408; Archaea.
DR HOGENOM; CLU_123700_0_0_2; -.
DR OMA; ITYYYLA; -.
DR OrthoDB; 109783at2157; -.
DR PhylomeDB; O30273; -.
DR EvolutionaryTrace; O30273; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9575239"
FT CHAIN 2..175
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT epsilon 2"
FT /id="PRO_0000155087"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1YTL"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1YTL"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:1YTL"
SQ SEQUENCE 175 AA; 19702 MW; 26CA5B99DB3135D5 CRC64;
MAKALEQPFD VANIPGPKMA TLLEKGKPVA NMIKKAKRPL LIVGPDMTDE MFERVKKFVE
KDITVVATGS AITRFIDAGL GEKVNYAVLH ELTQFLLDPD WKGFDGQGNY DLVLMLGSIY
YHGSQMLAAI KNFAPHIRAL AIDRYYHPNA DMSFGNLWKK EEDYLKLLDE ILAEL
