ID   PATR_STRGG              Reviewed;         359 AA.
AC   B1VP97;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Putative phenylalanine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01513};
DE            EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_01513};
GN   Name=pat {ECO:0000255|HAMAP-Rule:MF_01513}; OrderedLocusNames=SGR_3647;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: May catalyze the transamination reaction in phenylalanine
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01513}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01513};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255|HAMAP-Rule:MF_01513}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009493; BAG20476.1; -; Genomic_DNA.
DR   RefSeq; WP_012380056.1; NC_010572.1.
DR   AlphaFoldDB; B1VP97; -.
DR   SMR; B1VP97; -.
DR   STRING; 455632.SGR_3647; -.
DR   PRIDE; B1VP97; -.
DR   EnsemblBacteria; BAG20476; BAG20476; SGR_3647.
DR   GeneID; 6209659; -.
DR   KEGG; sgr:SGR_3647; -.
DR   PATRIC; fig|455632.4.peg.3715; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR   HAMAP; MF_01513; Phe_aminotrans_2; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR024892; Pat.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..359
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_1000146152"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   359 AA;  38332 MW;  C8FD1B514719CD9C CRC64;
     MSETSPKLRA ELDGVPAYVP GKPAAAGGPV AYKLSSNENP YPPLPGVLES ALAAAGSFNR
     YPDMACTGLM NELADRFGVP LGHLATGTGS VGVAQQLLQA TSGPGDEVIY AWRSFEAYPI
     ITQVSGATSV KVPLTDGEVH DLDAMAEAIT DRTRLIFVCN PNNPTGTVVR RAELERFLDR
     VPSDVLVVLD EAYKEFIRDA EVPDGIEIYR DRPNVAVLRT FSKAYGLAGL RVGFAVAHEP
     VAAALRKTAV PFGVSQLAQD AAVASLRAED ELLGRVGSLV AERTRVSAEL TRQGWTVPES
     HANFVWLRLG ERTLDFAGAC ERAGVVVRPF QGEGVRVSIG EGEGNDLFLK AAEAFRAEL