ID D2RGD1_ARCPA Unreviewed; 663 AA.
AC D2RGD1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN OrderedLocusNames=Arcpr_0286 {ECO:0000313|EMBL:ADB57356.1};
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB57356.1, ECO:0000313|Proteomes:UP000001901};
RN [1] {ECO:0000313|EMBL:ADB57356.1, ECO:0000313|Proteomes:UP000001901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC {ECO:0000313|Proteomes:UP000001901};
RX PubMed=21304717;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
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; CP001857; ADB57356.1; -; Genomic_DNA.
DR RefSeq; WP_012939692.1; NC_013741.1.
DR AlphaFoldDB; D2RGD1; -.
DR STRING; 572546.Arcpr_0286; -.
DR PaxDb; 572546-Arcpr_0286; -.
DR GeneID; 8738939; -.
DR KEGG; apo:Arcpr_0286; -.
DR eggNOG; arCOG01338; Archaea.
DR eggNOG; arCOG01340; Archaea.
DR HOGENOM; CLU_007415_3_1_2; -.
DR OrthoDB; 50180at2157; -.
DR Proteomes; UP000001901; 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; IPR043938; Ligase_CoA_dom.
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; PF19045; Ligase_CoA_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:UP000001901}.
FT DOMAIN 462..498
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 663 AA; 72695 MW; 863E71AB4D262288 CRC64;
MEELFEPRAI AVIGATPKEG KVGNTLLKNL SKFKGKIYAV NPKYREVLGV ECYPSVKDLP
EEVDLAVIAV PAEVVPKVLE ECGEKGVKAA VVISAGFREV GNYKLEMELV EICKKYGIKM
VGPNCLGIIN TSNGLNATFS GVEPLRGRIA LISQSGALIV AIMDWALANN IGFSKIVSLG
NKALLNECDF IEYLSNDDET EVIALYVEGI EEGRRFMEIA EKCRKPIVAI KSGKTSAGAK
AVSSHTGSLA GSYEACRTAF RQSGVVEAES VEELFDFSTV LSYIKGFRGG VAIVTNSGGP
AVMASDAVEK YNLNLASFEH ETVEMLRSIA PYGNVYNPVD VLGDADAERF CKALDIVAKD
RNVGLILAIL TPTATIDGVK VAEKIVGINK KVVGCFMGGK SFEEAVRILR EKGIANFNDP
VRAVKAIASV QFYSRRTKRK EFVRFDVDLK KVRELLKRGL YFEVVREYGI PVPPYGIARS
AEEALEIADK IGYPVAMKVV SPKIIHKTDV GCVKLNVTRN EVVKIFYEIL KRAEEFGDVE
GVMIQKMMPT GKEVIVGMKR DPSFGPLVMF GMGGIYVDVF RDVSFRIAPI SREDAEEMVR
EVKAYRILQG VRGEKPSDVD AIIDVILRVS QMVMDLEEIL ELDINPIFVY EKGCCAVDVK
VIV
//
