ACDG_ARCFU
ID ACDG_ARCFU Reviewed; 470 AA.
AC O29871;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000255|HAMAP-Rule:MF_01136};
DE Short=ACDS complex subunit gamma {ECO:0000255|HAMAP-Rule:MF_01136};
DE EC=2.1.1.245 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=ACDS complex methyltransferase {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=Corrinoid/iron-sulfur component large subunit {ECO:0000255|HAMAP-Rule:MF_01136};
GN Name=cdhE {ECO:0000255|HAMAP-Rule:MF_01136}; OrderedLocusNames=AF_0376;
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 1-19.
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). {ECO:0000255|HAMAP-
CC Rule:MF_01136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid
CC Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid
CC Fe-S protein] + H(+); Xref=Rhea:RHEA:45196, Rhea:RHEA-COMP:11110,
CC Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378, ChEBI:CHEBI:59924,
CC ChEBI:CHEBI:64267, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035;
CC EC=2.1.1.245; Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- SUBUNIT: Heterodimer of delta and gamma chains. The ACDS complex is
CC made up of alpha, epsilon, beta, gamma and delta chains with a probable
CC stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
CC {ECO:0000255|HAMAP-Rule:MF_01136}.
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DR EMBL; AE000782; AAB90860.1; -; Genomic_DNA.
DR PIR; H69296; H69296.
DR RefSeq; WP_010877883.1; NC_000917.1.
DR AlphaFoldDB; O29871; -.
DR SMR; O29871; -.
DR STRING; 224325.AF_0376; -.
DR DNASU; 1483591; -.
DR EnsemblBacteria; AAB90860; AAB90860; AF_0376.
DR GeneID; 24793915; -.
DR KEGG; afu:AF_0376; -.
DR eggNOG; arCOG01979; Archaea.
DR HOGENOM; CLU_050002_0_0_2; -.
DR OMA; SCMAFAT; -.
DR OrthoDB; 31154at2157; -.
DR PhylomeDB; O29871; -.
DR BioCyc; MetaCyc:AF_RS01920-MON; -.
DR BRENDA; 2.1.1.245; 414.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.20; -; 1.
DR HAMAP; MF_01136; CdhE; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR InterPro; IPR016218; AcylCoA_decarb/synth_gsu.
DR InterPro; IPR023427; AcylCoA_decarb/synth_gsu_arc.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR Pfam; PF03599; CdhD; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cobalt; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Methyltransferase; Reference proteome; Transferase.
FT CHAIN 1..470
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma"
FT /id="PRO_0000155118"
FT DOMAIN 1..62
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
SQ SEQUENCE 470 AA; 52551 MW; 0BEC4537F265CA3A CRC64;
MKVKSPLEVY NYLPRTNCGE CGFDTCMSFA AHILDRSVTP LDCKPLVRDA EKDPKVKKKL
EELLELTAPE IAEVVIGVGE NAVKIGGEEV LHRHELTFFN PTGFFYDVWD TMDDKALEER
CDRVVSYKKF YVGNFLTLDG FAVRCTSGDP KRYREVVKKV ASYGKPLILV ALDSECMKAA
LEEVADQRPL MYAATEGNWK EFLKLALEYK VPVTLRAKDL DLLKSMAVTF KQAGVKDIVL
DPVTEPLGEG LKGTFERVIQ LRRTAIAGQD KDVAYPIMIT PIAAWLIEGD DVTKSYWEAV
IASIFIVKYG DVMIFRSIDQ HVVMPTITLR FNIYTDPRTP VQVEPGLRAI NDPGPDDPVF
ITTNFALTYY TVESDLTSGG IKGWLLVLNT EGLGVEVSVA GGQFTASKVK ELIEETKIEE
KVNHRYLVIP GLAARLQGAI EDETGWKVLV GPMDSGRIKG WLEKNWPPKE
