ID   Q1I9Z5_PSEE4            Unreviewed;       377 AA.
AC   Q1I9Z5;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Serine-pyruvate transaminase {ECO:0000313|EMBL:CAK15526.1};
DE            EC=2.6.1.51 {ECO:0000313|EMBL:CAK15526.1};
GN   OrderedLocusNames=PSEEN2741 {ECO:0000313|EMBL:CAK15526.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK15526.1, ECO:0000313|Proteomes:UP000000658};
RN   [1] {ECO:0000313|EMBL:CAK15526.1, ECO:0000313|Proteomes:UP000000658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48 {ECO:0000313|EMBL:CAK15526.1,
RC   ECO:0000313|Proteomes:UP000000658};
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR000524-50};
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DR   EMBL; CT573326; CAK15526.1; -; Genomic_DNA.
DR   RefSeq; WP_011533921.1; NC_008027.1.
DR   AlphaFoldDB; Q1I9Z5; -.
DR   STRING; 384676.PSEEN2741; -.
DR   GeneID; 32805882; -.
DR   KEGG; pen:PSEEN2741; -.
DR   eggNOG; COG0075; Bacteria.
DR   HOGENOM; CLU_044792_0_0_6; -.
DR   OrthoDB; 9766472at2; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0004760; F:serine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR   PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR   PIRSF; PIRSF000524; SPT; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000313|EMBL:CAK15526.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000524-50}; Pyruvate {ECO:0000313|EMBL:CAK15526.1};
KW   Transferase {ECO:0000313|EMBL:CAK15526.1}.
FT   BINDING         348
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT   MOD_RES         197
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ   SEQUENCE   377 AA;  40831 MW;  09087D24E5D556AA CRC64;
     MSKIYPGIDP EGLVEYSVVY TDRSLNHMSQ SFQGVMKNIS TTLKQVYNAQ AVAVVPGSGT
     FGMEAVARQF ATGQQCLVIR NGWFSYRWSQ ILEMGNIPAA TTVLKARPVE TGRQAAYAPA
     PLDEVLAAIA SQKPQIVFAP HVETSSGIIL PDEYLRAVGD AVHAVGGLFV LDCIASGAIW
     VDMHKCAVDL LISAPQKGWS ASPCCALVML STLALERIES TQSTSFACDL KKWLQIMLAY
     EQGGHAYHAT MPSDALARFN EVMKETQAYG FDKVCDEQQA LGDRVRAMMA RKGIKSVAAA
     GFQAPGVVVS YTDDADIKSG KKFVSHGLQI AAGVPLQCDE PADFQTFRIG LFGLEKLHNL
     ERTVSTLEQA LDEVMVN
//