ID   A0A1G8M4E3_9PSED        Unreviewed;       694 AA.
AC   A0A1G8M4E3;
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:SDI62765.1};
GN   ORFNames=SAMN05216272_11369 {ECO:0000313|EMBL:SDI62765.1};
OS   Pseudomonas panipatensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=428992 {ECO:0000313|EMBL:SDI62765.1, ECO:0000313|Proteomes:UP000199636};
RN   [1] {ECO:0000313|EMBL:SDI62765.1, ECO:0000313|Proteomes:UP000199636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 7469 {ECO:0000313|EMBL:SDI62765.1,
RC   ECO:0000313|Proteomes:UP000199636};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNDS01000013; SDI62765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8M4E3; -.
DR   STRING; 428992.SAMN05216272_11369; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000199636; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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; 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; 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          487..537
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   694 AA;  72847 MW;  A8EC11C7DB29CBF2 CRC64;
     MKRENLQRLL APRHLAFIGG RSMARALKRC AEGGFAGPLW LVNPQYDELE GVPCVRSIAA
     LPEGPDAVFV ATNRELTLQA VAELAAKGAG GAICYASGFA ETGAEGQALQ QQLLAAAGDM
     ALLGPNCYGL LDYLHGAALW PVAHGGQRVE KGVAVLTQSG NFAYNLSMSD RSLPIAYMAS
     VGNQAQLGVA ELMDVLLDEP RVTAIGLHLE GLKNVPGFAR AAYKALQKGI PLIALKTGVS
     QIGAELALSH TSSLAGSDAL YDSLFERLGV IRVSGPVSFI ETLKAAACGN LPGGPRLAAL
     ACSGGDAGLI ADYAERNGLS LPPLSEAQRL ALAEVLPDYA NIANPLDFTT AIWGDGAALE
     RMLDSALRTP ADAALLVLDY PGEETGERPQ CDLLLELYCA ALARHGKVGF IASALPELLP
     AHARERLHGH GVAALQGVED GLAAWGRIAH YRQRREALLA RGEAALVPLC PQAVEGEGRL
     LDEWQSKQAL KAFGLPLPAA VLSTPRQARE AAADLGYPLV LKAVSVELPH KTEAGGVALN
     LRNEAALEAA LFDMRESLAK HAPQVPFDQV LLERMASPPL AELIIGIKRE VGFGLALVLG
     AGGILVELLK DSRSLLLPTT DAAIRDALLS LRSAPLLSGF RGRPAVDMDA LVDAIRAVAD
     YACEHVDSLL ELDVNPLLVN AEGAVAVDAL VRLG
//