ACDB2_METJA
ID ACDB2_METJA Reviewed; 469 AA.
AC Q57620;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2;
DE Short=ACDS complex subunit beta 2;
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase 2;
GN Name=cdhC2; OrderedLocusNames=MJ0156;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 complex generates CO from CO(2), while the beta subunit (this protein)
CC combines the CO with CoA and a methyl group to form acetyl-CoA. The
CC methyl group, which is incorporated into acetyl-CoA, is transferred to
CC the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta
CC complex). {ECO:0000255|HAMAP-Rule:MF_01138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA
CC + methyl-Co(III)-[corrinoid Fe-S protein]; Xref=Rhea:RHEA:45212,
CC Rhea:RHEA-COMP:11110, Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.3.1.169;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01138};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; Evidence={ECO:0000250};
CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000250};
CC -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, beta,
CC gamma and delta chains with a probable stoichiometry of
CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}.
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DR EMBL; L77117; AAB98138.1; -; Genomic_DNA.
DR PIR; E64319; E64319.
DR RefSeq; WP_010869651.1; NC_000909.1.
DR AlphaFoldDB; Q57620; -.
DR SMR; Q57620; -.
DR STRING; 243232.MJ_0156; -.
DR EnsemblBacteria; AAB98138; AAB98138; MJ_0156.
DR GeneID; 1451000; -.
DR KEGG; mja:MJ_0156; -.
DR eggNOG; arCOG04360; Archaea.
DR HOGENOM; CLU_613408_0_0_2; -.
DR InParanoid; Q57620; -.
DR OMA; FMHLNQR; -.
DR OrthoDB; 26992at2157; -.
DR PhylomeDB; Q57620; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR Gene3D; 3.30.1650.10; -; 1.
DR HAMAP; MF_01138; CdhC; 1.
DR InterPro; IPR045822; ACS_CODH_B_C.
DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR InterPro; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc.
DR InterPro; IPR011254; Prismane-like_sf.
DR PANTHER; PTHR42281; PTHR42281; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR00316; cdhC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Iron; Iron-sulfur; Metal-binding; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..469
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 2"
FT /id="PRO_0000155102"
FT BINDING 187
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 190
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 276
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 278
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
SQ SEQUENCE 469 AA; 52642 MW; BDC866AD7C28661C CRC64;
MFDDIPVSVG PMNEGERVRG PDMYVELAGP KSYGFELVKV VNKAEDKVEI IGKDIDEMEE
GSRNPFAIIV EVSGSNLEED LEGVLERRIH EFLNYIEGVM HLNQRDQVWI RINKDSFNKG
LRLKHIGKVV QRLFKAEFPF IEKCDVTIIT DPEKVKEELE KAREIYNKRD EKTKALHEED
VDVFYGCVMC QSFAPTHVCV ITPDRPALCG GINYLDARAA AKIDPNGPIF EIPKGECLDE
KLGIYSGVNE VVRERSQGTV EEVTLHSALE KPCTSCGCFE AIVFYIPEVD GFGIAHRGYK
GETPMGIPFS TLAGQCSGGK QVPGFVGISI SYMKSPKFLQ GDGGWERVVW LPKELKERVK
DAIPEELYDK IATEEDVKTT DELIKFLKEK GHPCAERIGA EVEEEAIEEE EVEEEMEEVE
GIEVPTMTLP GTFAGLPPGI KIVLYNAVIK AEKIIITKEE PEKKKKKKK
