ID   PATR_CORGB              Reviewed;         341 AA.
AC   A4QAL4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=cgR_0297;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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}.
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DR   EMBL; AP009044; BAF53261.1; -; Genomic_DNA.
DR   RefSeq; WP_011896550.1; NC_009342.1.
DR   AlphaFoldDB; A4QAL4; -.
DR   SMR; A4QAL4; -.
DR   EnsemblBacteria; BAF53261; BAF53261; cgR_0297.
DR   KEGG; cgt:cgR_0297; -.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   PhylomeDB; A4QAL4; -.
DR   Proteomes; UP000006698; 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..341
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_1000024493"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   341 AA;  36420 MW;  5D7B522674898CE3 CRC64;
     MIRADLATIP TYVPGRRLNN ATKLSSNEVS FSPLPAAVDA VTEATQGANR YPDMGAVELR
     EALAEHLEVE FDQVTVGCGS SALCQQLVQA TCAQGDEVIF PWRSFEAYPI FAQVAGATPV
     AIPLTADQNH DLDAMAAAIT DKTRLIFICN PNNPSGTTIT QAQFDNFMEK VPNDVVVGLD
     EAYFEFNRAD DTPVATEEIH RHDNVIGLRT FSKAYGLAGL RVGYAFGNAE IIAAMNKVAI
     PFAVNSAAQA AALASLNSAD ELMERVEETV EKRDAVVAAL GTAPTQANFV WLPGEGAAEL
     AAKLAEHGIV IRAFPEGARI SVTNAEETDK LLRAWEAINA G