ID   PATR_COREF              Reviewed;         342 AA.
AC   Q8FU28;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   25-MAY-2022, entry version 102.
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=CE0193;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAC17003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000035; BAC17003.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FU28; -.
DR   SMR; Q8FU28; -.
DR   STRING; 196164.23492028; -.
DR   EnsemblBacteria; BAC17003; BAC17003; BAC17003.
DR   KEGG; cef:CE0193; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   Proteomes; UP000001409; 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..342
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153511"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   342 AA;  36446 MW;  34D2B6340EE6FF01 CRC64;
     MIRADLTDIP TYVPGKNLGD ALKLSSNEVA FPPLPAAVSA ITEAATGANR YPDMGAVELR
     GVLADHLELT PEQITVGCGS SALCQQLVQA TCAAGDEVIF PWRSFEAYPI FARVAGATAV
     PIPLLPDTQG HDLEGMLDAI TDRTRLIFLC NPNNPSGTTF TEEQFEAFMQ RVPADVVVGL
     DEAYFEFNRA EDSPVSTEAV QRYPNVIGLR TFSKAYGLAG VRVGYAFGNP ELIGAMNKVA
     IPFAVSSLAQ AAAIASLNAA DELLERTEEV VTERERVAQV VGAAPSQANF VWLPGEGAAE
     LAGRLAEHGV VIRAFPEGAR ITVTNAAETD RLIRAWEAVH HG