ID O29075_ARCFU Unreviewed; 664 AA.
AC O29075;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 08-NOV-2023, entry version 116.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN OrderedLocusNames=AF_1192 {ECO:0000313|EMBL:AAB90053.1};
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 {ECO:0000313|EMBL:AAB90053.1, ECO:0000313|Proteomes:UP000002199};
RN [1] {ECO:0000313|EMBL:AAB90053.1, ECO:0000313|Proteomes:UP000002199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16
RC {ECO:0000313|Proteomes:UP000002199};
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.P., Clayton R.A., Tomb J., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M., 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., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B., Peterson S.,
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., Utterback T., 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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + ADP + phosphate;
CC Xref=Rhea:RHEA:15081, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456216; EC=6.2.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001619};
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DR EMBL; AE000782; AAB90053.1; -; Genomic_DNA.
DR PIR; G69398; G69398.
DR RefSeq; WP_010878688.1; NC_000917.1.
DR AlphaFoldDB; O29075; -.
DR STRING; 224325.AF_1192; -.
DR PaxDb; 224325-AF_1192; -.
DR EnsemblBacteria; AAB90053; AAB90053; AF_1192.
DR GeneID; 1484416; -.
DR KEGG; afu:AF_1192; -.
DR eggNOG; arCOG01338; Archaea.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_2_2_2; -.
DR OrthoDB; 18103at2157; -.
DR PhylomeDB; O29075; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR Pfam; PF13549; ATP-grasp_5; 1.
DR Pfam; PF13380; CoA_binding_2; 1.
DR Pfam; PF13607; Succ_CoA_lig; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000002199}.
FT DOMAIN 9..45
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 664 AA; 72907 MW; 23737948C90B4442 CRC64;
MLLLEHESKA LLEKYGIKTA KCIFCETEEQ AVKAAKEIGF PVVMKVAGRE IVHKSDVGGV
ILNVKSEDEV REVFQRLMSI PKAEGVNVQP QLEKGIEVIV GVAENEQFGS VAMFGLGGVF
VEVLKDVSFR LLPLTRRDAE EMVREVKGYK LLEGYRGVRG DVGAVVDLLL KLNEVVERES
IVEMDLNPVF VYERGAVVAD ARIVVGERKR FEMGVEDISF FFKAKSVAVI GASRNLLKPG
GRVLSNLKHL GFRGKVYPVN PNAGEILGYK CYPSVRAIPD KVDLAVIAVP SKNAIEVVKE
CAEKGVKGII VLSAGFAEGW EQGKELERQI VEIARKSGMR IVGPNTMGIL DPESGLTSFF
SVLRKIGQGN IGVLAQSGAV ANFILLPLWH VGFSKIVAIG NKADVGEVEV LNFLLKDEKT
RVVAAYLEGF TNGRKFYELM KASTKPIVVL KSGRTEAGKR SALSHTASIS TSEEIFEAAC
KQAGVAKVYD FEELVDAAKA LALQPLPRGT RVGVIQPSGA ECVMSADAVV ENGLELAKYS
EKTLERLYEL APEWHSINNP LDLYPIAEKS GDEVFNEVLK VFNEDENIDA IVAGVFIPSI
MKLGVDFSWT RKFSKPVLFT MKDDIEELRQ ARIEIERSGV PVYPTPERAV RALRHMVTVA
KRKS
//
