ID   PATR_NOCFA              Reviewed;         358 AA.
AC   Q5Z3C0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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}; Synonyms=hisC2;
GN   OrderedLocusNames=NFA_2290;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD55071.1; -; Genomic_DNA.
DR   RefSeq; WP_011206758.1; NC_006361.1.
DR   AlphaFoldDB; Q5Z3C0; -.
DR   SMR; Q5Z3C0; -.
DR   STRING; 247156.NFA_2290; -.
DR   EnsemblBacteria; BAD55071; BAD55071; NFA_2290.
DR   GeneID; 61131075; -.
DR   KEGG; nfa:NFA_2290; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   BioCyc; NFAR247156:NFA_RS01170-MON; -.
DR   Proteomes; UP000006820; 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..358
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153518"
FT   MOD_RES         219
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   358 AA;  38534 MW;  03A4D02A7EB24DE5 CRC64;
     MSARIRPDLS SIPAYTPGRS NPGAVKLASN ETTLPPLPAA AKAIAEAAEL AHRYPDNQSG
     ELRAALAEFL GVRVENVAIG CGSVALCQEL VQITCSSPRD EVLFAWRSFE AYPIITQVGN
     ATAVQVPLSP DYAHDLDALA AAVTEHTRLI FVCNPNNPTG TAHGRAALER FLDAVPAHVL
     VVLDEAYYEY MRLTPQDRPD GVEVGRNRPN VVVLRTFSKA YGLAGLRVGY AVGDPEVITA
     LMKVHIPFSV NRVAQAAAIA SLEARHELLE RTEAVIVERE RLREALLAAG YDVPPSETNF
     VWLPLGAHSA EFGEASAAAG VLVRPYGTDG VRVTVGDPHE NEMFLRFAAD PAVVARFR