ID A0A0A1VDF0_9BURK Unreviewed; 707 AA.
AC A0A0A1VDF0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:GAD21164.1};
GN ORFNames=AVS7_00924 {ECO:0000313|EMBL:GAD21164.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD21164.1};
RN [1] {ECO:0000313|EMBL:GAD21164.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD21164.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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DR EMBL; DF238899; GAD21164.1; -; Genomic_DNA.
DR RefSeq; WP_020227219.1; NZ_DF238899.1.
DR AlphaFoldDB; A0A0A1VDF0; -.
DR STRING; 1268622.AVS7_00924; -.
DR eggNOG; COG1042; Bacteria.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000030646; Unassembled WGS sequence.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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:UP000030646}.
FT DOMAIN 496..532
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 707 AA; 74697 MW; 65C0E1D984D8E951 CRC64;
MTTNAHHPQR LQPLLAPRSI ALIGASDNPG RIGGMPLDLL RHFGFAGAVY PVNPKYQEVF
GYRCYPDIES LPEACDLVVL AIAAPEVTAM LERCHARGIP AGIVYAAGFA EAPGEGEALQ
RTLEAFVQRS GMVVAGPNCM GFANLNLHAY TAFASVFKNV PPQTGPGRAS IVTQSGNVCS
AVFALARRLG VPVSHFINTG NEACVEFSEY LQYLAADEST ECVVGYVEQL RDGPRFIDAA
LAFARQRKPL ILYKAGETDK GSEAVRSHTS ALAGDLALYK AAFEQLNVIR GTDFAQMADL
AYLSGFRARQ GGPRVAIVTM SGALGAILAD KFIGAGLEVP TLSEDLQHTL REGIPDYGMV
SNPVDVTGNV VNSPQFVRTI LGALAQSDQV DTVVVYAPGY LLDRMAEPLV EVCGQWNKLF
VAIDTGAARC RDQLAQASVP VFDDIGRATQ ALAPFCQWLA RHEDVARWAA LRQAQAVVQQ
GAAPALPAAL NEHATKLLLA GYGVPSLQGL PARDADEAVA AAGQLGYPVA LKILSADIAH
KTEVGGVRLN VADDAALRTL CADMLASVQR HSPAARIDGF LVQPMASGGV AELIAGITHD
PVFGPALTVG LGGVLTELYR DASHRLLPVD AAMVQTMLRG LRAWPLLDGF RGRPLADVDG
ACEGIAALSR AQAALGPQVQ EIEINPLQVR AQGQGAFALD ALVVVQG
//