ACDB1_METJA
ID ACDB1_METJA Reviewed; 748 AA.
AC Q57616;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 1;
DE Short=ACDS complex subunit beta 1;
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase 1;
GN Name=cdhC1; OrderedLocusNames=MJ0152;
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; AAB98134.1; -; Genomic_DNA.
DR PIR; A64319; A64319.
DR AlphaFoldDB; Q57616; -.
DR SMR; Q57616; -.
DR STRING; 243232.MJ_0152; -.
DR PRIDE; Q57616; -.
DR EnsemblBacteria; AAB98134; AAB98134; MJ_0152.
DR KEGG; mja:MJ_0152; -.
DR eggNOG; arCOG02428; Archaea.
DR eggNOG; arCOG04360; Archaea.
DR HOGENOM; CLU_378422_0_0_2; -.
DR InParanoid; Q57616; -.
DR OMA; GPNQPIP; -.
DR PhylomeDB; Q57616; -.
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 Gene3D; 3.40.50.2030; -; 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; IPR041350; CODH_A_N.
DR InterPro; IPR016099; Prismane-like_a/b-sand.
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 Pfam; PF18537; CODH_A_N; 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..748
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 1"
FT /id="PRO_0000155101"
FT BINDING 480
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 483
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 569
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 571
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
SQ SEQUENCE 748 AA; 82957 MW; 3BD5E42A4ABA3E8E CRC64;
MKIRLYGETM VVGNIIEGGK TVLNLTKEIL EKEDENLKVS YPGTNYNLPI IYGLLGKKIE
TVKDLKELIN SLEIKDEETL ENALDAGVVT LICAEAIEAL KYAKSEKPYK EPYVGFIPDE
ILRGLGVPLV EGKIPAILVV IGKVGDKEKL KKLIDDIKKR NILALLVGDI VKEMDEADIE
YGLDKLLVPV GNEITSAIHA ANLAIRAPLI FGGIEPGKTE EIIDYLKNRV PAVVVALGEL
DNITLAAGAG CIKAGVPVIT NNEVPVIKGA LESSDIDNIV ENALKMKGVK VKVVEFDIPV
SVGPMNEGER VRGPDMYVEL AGPKSYGFEL VKVVNKAEDK VEIIGKDIDE MEEGSRNPFA
IIVEVSGSNL EEDLEGVLER RIHEFLNYIE GVMHLNQRDQ VWIRINKNSF NKGLRLKHIG
EVVKQLFKEH FPIVEKCNVI IITDPDKVKE ELEKAKEIYK KRDEKTKSIR EEDVDVFYGC
VMCQSFAPTH VCIITPDRPS LCGSINYLDA RAAAKIDPNG PIFEIPKGEC LDEKLGIYTG
VNEVVRERSQ GSVEEMALHS ALTNPCTSCG CFEAIVFYIP EVDGFGVAHR NFRGETPFGL
PFSTLAGQCS GGKQVPGFVG ISISYMKSPK FLQGDGGWER VVWLPKELKE RVKDAIPEEL
YDKIATEEDV KTTDELIKFL KEKGHPIVKK TEEEVVEEVE EEKEEVKATE EEKEGIEVGE
LITKLAKEGG IQIIMKNVKI VINLNVKR
