ID   A0A1I4NTB2_9BURK        Unreviewed;       710 AA.
AC   A0A1I4NTB2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Acyl-CoA synthetase (NDP forming) {ECO:0000313|EMBL:SFM18600.1};
GN   ORFNames=SAMN05444747_103218 {ECO:0000313|EMBL:SFM18600.1};
OS   Variovorax sp. OV329.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM18600.1, ECO:0000313|Proteomes:UP000199688};
RN   [1] {ECO:0000313|EMBL:SFM18600.1, ECO:0000313|Proteomes:UP000199688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV329 {ECO:0000313|EMBL:SFM18600.1,
RC   ECO:0000313|Proteomes:UP000199688};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOUG01000003; SFM18600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4NTB2; -.
DR   STRING; 1882825.SAMN05444747_103218; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000199688; 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:UP000199688}.
FT   DOMAIN          492..528
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   710 AA;  73690 MW;  5C8B02B6B1C2FBFA CRC64;
     MDIGRGLDAV FQPRSIAIFG ASDDATKIGG RPLQFLQKYG YAGAIYPINR KGGVVQTLPA
     YASVAEVPEA PDLAVVAVPP EGVLDVVRDC ARRGVRAAVI LSSGFSEMGE AGSRLQSQIS
     QVARDSGMRV VGPNCLGAIG IAEKSIATFS VALESAMPAA GNVGIVSQSG NLGSFTMRLA
     AERGVGISRL LTTGNECDVD IADGIASLAG DVSTSVILCC METCRDGERF VKALDLAREA
     GKAVVVLKVG VSEAGSEAAA SHTGALAGSD AVFDAVLRRA GALRVPSIEQ LLEVGHAIAV
     VGRQRLPHGG RTALITASGG FGVLLADAAS AQGLELPKLS QETRERILSV LPYASPANPV
     DMTAQVSSKP ELLAQVLNAV AEDPVCDALI LQSAAAFHVP RLRDTYIAAL RQVREKHPDR
     LILLCCRGPR EVLAQLNAMG LPTVEGIDAA CATVAALVKL GKNQSRAETA AVSLQDLPPL
     ADAAFEDEAN AKAALGQAGL PMLREQVVQS LPQALDFAGG IGFPVVLKIV SPDIAHKTEV
     GGVVVGVQSE SQLRTEYGAL LERVAVKAPR ARITGVLVAQ MARGGTELIL GTKKDPVFGP
     VVMVGLGGIF AEVLRDVALE TAPVDEAQAL AMLRSLKAFA LLDGARGRPK ADVQAAAQAI
     VKLSRFAARH ADRVTEIDIN PLLVQDQGQG AWALDALLVR ESAGANKKDE
//