ID U1PPU1_9EURY Unreviewed; 711 AA.
AC U1PPU1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=acetate--CoA ligase (ADP-forming) {ECO:0000256|ARBA:ARBA00012957};
DE EC=6.2.1.13 {ECO:0000256|ARBA:ARBA00012957};
GN ORFNames=J07HB67_01445 {ECO:0000313|EMBL:ERH12426.1};
OS halophilic archaeon J07HB67.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales.
OX NCBI_TaxID=1085029 {ECO:0000313|EMBL:ERH12426.1};
RN [1] {ECO:0000313|EMBL:ERH12426.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(2013).
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE356582; ERH12426.1; -; Genomic_DNA.
DR AlphaFoldDB; U1PPU1; -.
DR STRING; 1085029.J07HB67_01445; -.
DR HOGENOM; CLU_007415_3_1_2; -.
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}.
FT DOMAIN 486..522
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 711 AA; 73612 MW; F9041AA4C50BA621 CRC64;
MTDAGLFAPD RVAVVGATER EGSVGRAVTA NLLADFDGEV VPVNPSRETV LGEPCVASVG
DSGADLAIVA VPPAIAVETV REAGEHGIDN LVVLTAGFGE TGSEGAARER QLREIAAEYD
LTLVGPNSLG VASTPVGLNG TFGPSMPDSG SISFMSQSGA FVTAVIDWAF EQDIGFRHVV
SLGNKTVVDE TDLVGDWGAD DGTDVIVGYL ESVVDGEAFV ETAREVTSDT PVVVIKSGRT
EAGAGAAASH TGAIAGNERA YEVGLREAGV LRAESAGELF DAARALAGQP LPETDGVAVV
TNAGGPGVMA TDAVGDAESL SLADLSDETV DALAESLPAE ANRFNPVDVI GDADADRFRE
ALRVTLADDG VGACVVIAAP TATLSFDALA AAVVDVQRDT DLPIAACLMG GEQASASSET
LSEAGVPTYF DPSRAVGSLD TLGRYREVQE RETGKPERFD VDRDRVHEIL SRVRDRPDNR
LGVESMAILD AYGVPTPDGE IVDDPERAAT VATGIDGPVV MKIVSPDILH KSDIGGVAVG
VADDEVTDTY ERLVTRARNY QPDATILGVQ VQAAVDLDTG VETIVGISRD PQFGPLVVFG
LGGIFVETLE DTAASLAPVD ESTARGMTEE IDAAPLLRGA RGRDPTDLDA VVETIQRLSQ
LAADFPSIVE LDVNPLVAGP DGVTAIDLQL TVDPETLPSR GDTNQPHGDD R
//
