ID   PATR_CORJK              Reviewed;         373 AA.
AC   Q4JSJ5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=jk2030;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI38212.1; -; Genomic_DNA.
DR   RefSeq; WP_011274301.1; NC_007164.1.
DR   AlphaFoldDB; Q4JSJ5; -.
DR   SMR; Q4JSJ5; -.
DR   STRING; 306537.jk2030; -.
DR   EnsemblBacteria; CAI38212; CAI38212; jk2030.
DR   KEGG; cjk:jk2030; -.
DR   PATRIC; fig|306537.10.peg.2062; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   Proteomes; UP000000545; 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; Reference proteome; Transferase.
FT   CHAIN           1..373
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153513"
FT   MOD_RES         212
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   373 AA;  39304 MW;  0336CA8713EB5543 CRC64;
     MIRPDLSSLP AYVPGSTQPG ALKLASNESS LSPLPSVSAV INDATSNLNR YPDMASGALR
     GKLAQWLGVD LDNVAVGNGS SALCQQLVQA TCKDGDEVVY AWRSFEAYPI LCKIAGAVGV
     GVPLKSGRHD LKAMSEAIGE RTRLVFVCNP NNPTGTTVSR DEFREFMGRV PADVTVVLDE
     AYVEYNRDAE SPVALEELQR YPNLAVCRTF SKAYGLAGLR LGYLVGPAEL VEAVNKVGIP
     FGVNALAQAA GIASVEAQGE LAERVDATVA ERERVEAYLA GVAPAGADEP LTYPSQANFV
     WLNAGERAEA LDEALKREGV IARCFAGEGV RVTVTTAEET DVLLRALERA LPAVGLVEAG
     AESAGLQASP QAD