ACDE1_METBF
ID ACDE1_METBF Reviewed; 170 AA.
AC Q46G05;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
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 {ECO:0000255|HAMAP-Rule:MF_01134};
GN OrderedLocusNames=Mbar_A0203 {ECO:0000312|EMBL:AAZ69187.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, SUBUNIT, INDUCTION, AND PATHWAY.
RC STRAIN=MS;
RX PubMed=6425262; DOI=10.1128/jb.158.1.231-237.1984;
RA Krzycki J.A., Zeikus J.G.;
RT "Characterization and purification of carbon monoxide dehydrogenase from
RT Methanosarcina barkeri.";
RL J. Bacteriol. 158:231-237(1984).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACDS ALPHA SUBUNIT,
RP AND SUBUNIT.
RX PubMed=18621675; DOI=10.1073/pnas.0800415105;
RA Gong W., Hao B., Wei Z., Ferguson D.J., Tallant T., Krzycki J.A.,
RA Chan M.K.;
RT "Structure of the alpha2epsilon2 Ni-dependent CO dehydrogenase component of
RT the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9558-9563(2008).
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 (PubMed:6425262). The precise role of the epsilon subunit
CC is unclear; it may have a stabilizing role within the
CC alpha(2)epsilon(2) component and/or be involved in electron transfer to
CC FAD during a potential FAD-mediated CO oxidation (PubMed:18621675).
CC {ECO:0000255|HAMAP-Rule:MF_01134, ECO:0000269|PubMed:6425262,
CC ECO:0000305|PubMed:18621675}.
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000255|HAMAP-Rule:MF_01134, ECO:0000305|PubMed:6425262}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits
CC (PubMed:6425262). The ACDS complex is made up of alpha, epsilon, beta,
CC gamma and delta subunits with a probable stoichiometry of
CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_01134, ECO:0000269|PubMed:6425262,
CC ECO:0000305|PubMed:18621675}.
CC -!- INDUCTION: Up-regulated during growth on acetate.
CC {ECO:0000269|PubMed:6425262}.
CC -!- SIMILARITY: Belongs to the CdhB family. {ECO:0000255|HAMAP-
CC Rule:MF_01134}.
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DR EMBL; CP000099; AAZ69187.1; -; Genomic_DNA.
DR RefSeq; WP_011305242.1; NC_007355.1.
DR PDB; 3CF4; X-ray; 2.00 A; G=1-170.
DR PDBsum; 3CF4; -.
DR AlphaFoldDB; Q46G05; -.
DR SMR; Q46G05; -.
DR STRING; 269797.Mbar_A0203; -.
DR EnsemblBacteria; AAZ69187; AAZ69187; Mbar_A0203.
DR GeneID; 3626294; -.
DR KEGG; mba:Mbar_A0203; -.
DR eggNOG; arCOG04408; Archaea.
DR HOGENOM; CLU_123700_0_0_2; -.
DR OMA; PYYLSRM; -.
DR OrthoDB; 109783at2157; -.
DR UniPathway; UPA00642; -.
DR EvolutionaryTrace; Q46G05; -.
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 3D-structure; Methanogenesis.
FT CHAIN 1..170
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT epsilon 1"
FT /id="PRO_0000436852"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3CF4"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3CF4"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3CF4"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:3CF4"
SQ SEQUENCE 170 AA; 18555 MW; 63B0B42CE31EAD2A CRC64;
MVDTTKNTKL FTSYGVSTSR TVSPEMAAKL ISKAKRPLLM VGTLTLEPEI LDRVVKISKA
ANIPIAATGS SMASLVDKDV DAKYINAHML GFYLTDPKWP GLDGNGNYDM VIAIGFKKYY
INQVLSAAKN FSNLKTIAIE RGYIQNATMS FGNLSKADYY AALDELINAL
