ID   U2A1V1_9PSED            Unreviewed;       697 AA.
AC   U2A1V1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:ERI53323.1};
GN   ORFNames=N878_15850 {ECO:0000313|EMBL:ERI53323.1};
OS   Pseudomonas sp. EGD-AK9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI53323.1, ECO:0000313|Proteomes:UP000016488};
RN   [1] {ECO:0000313|EMBL:ERI53323.1, ECO:0000313|Proteomes:UP000016488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA   Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA   Purohit H.J.;
RT   "Indian agricultural soil isolates capable of pesticide degradation.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERI53323.1}.
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DR   EMBL; AVOF01000111; ERI53323.1; -; Genomic_DNA.
DR   RefSeq; WP_021442806.1; NZ_AVOF01000111.1.
DR   AlphaFoldDB; U2A1V1; -.
DR   PATRIC; fig|1386078.3.peg.1180; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000016488; 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          488..538
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   697 AA;  72870 MW;  25FA70A97B06C8FF CRC64;
     MSLHNNIRRL LAPKHLAFIG GRSMARALKR CAEGGFGGQL WLVNPQHAEL EGVPCVASIR
     ELPCGPDAVF IATNRELTLQ AVAELAAKGA GGAICYASGF AETGEAGERL QAELLRAAGY
     MALLGPNCYG LLDYLHGAAL WPVAHGGQRV ERGVAVLTQS GNFAYNLSMS DRSLPVAYMA
     SVGNQAQLGV AELMDALLDE PRVTAIGLHL EGLKNIPGFA RAAYKALVKG IPIIALKTGV
     SQIGAELALS HTSSLAGSDA LYDALFQRLG VIRVSGPVSF METLKAAACG RLPAGPGLIA
     LACSGGDAGL IADYAEANGL ALPKLDETQR LELAEVLPAY ANIANPLDFT TAIWGDAQAL
     TRMLDSCLSR PADAALLVLD YPDEQSGERP QCDLLLELYC DALARHGKSG FIASAFPELL
     PAQARDYLHA RGVPALQGVE DGLAAWGRIA DYQSRRQALL AMGEAALVPL ATGSAVVTGG
     LLDEWQSKQA LGAFGLPLPR GVLSTPECAL ADAEQLGYPL VLKAVSAELP HKTEAGGVAL
     NLRDAGQLQS ALERMRRDLA EHAPTLAFDQ VLLEAMASPP LAELIVGVKR EPGFGLALVL
     GAGGILVELL RDSRSLLLPT NPAAIRQALL GLRSAPLLSG FRGRPAADLD ALVAAIGAVA
     DYACEHAERL LELDVNPLLV GAHGCVAVDA LIRLAQD
//