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Database: UniProt
Entry: A0A0A1VDF0_9BURK
LinkDB: A0A0A1VDF0_9BURK
Original site: A0A0A1VDF0_9BURK 
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
//
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