ID   PATR_CORGL              Reviewed;         341 AA.
AC   Q8NTT4;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable phenylalanine aminotransferase;
DE            EC=2.6.1.-;
GN   Name=pat; OrderedLocusNames=Cgl0218, cg0267;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948641; DOI=10.1016/s0168-1656(03)00161-5;
RA   McHardy A.C., Tauch A., Rueckert C., Puehler A., Kalinowski J.;
RT   "Genome-based analysis of biosynthetic aminotransferase genes of
RT   Corynebacterium glutamicum.";
RL   J. Biotechnol. 104:229-240(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: May catalyze the transamination reaction in phenylalanine
CC       biosynthesis.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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; AY238319; AAO92310.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB97611.1; -; Genomic_DNA.
DR   EMBL; BX927148; CAF18789.1; -; Genomic_DNA.
DR   RefSeq; NP_599471.2; NC_003450.3.
DR   RefSeq; WP_011013481.1; NC_006958.1.
DR   AlphaFoldDB; Q8NTT4; -.
DR   SMR; Q8NTT4; -.
DR   STRING; 196627.cg0267; -.
DR   DNASU; 1021282; -.
DR   KEGG; cgb:cg0267; -.
DR   KEGG; cgl:Cgl0218; -.
DR   PATRIC; fig|196627.13.peg.222; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   Proteomes; UP000000582; 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..341
FT                   /note="Probable phenylalanine aminotransferase"
FT                   /id="PRO_0000153512"
FT   MOD_RES         213
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   341 AA;  36450 MW;  5DC10FBEFFC1C67B CRC64;
     MIRADLATIP TYVPGRRLVD ATKLSSNEVS FSPLPAAVDA VTEATWGANR YPDMGAVELR
     EALAEHLEVE FDQVTVGCGS SALCQQLVQA TCAQGDEVIF PWRSFEAYPI FAQVAGATPV
     AIPLTADQNH DLDAMAAAIT DKTRLIFICN PNNPSGTTIT QAQFDNFMEK VPNDVVVGLD
     EAYFEFNRAD DTPVATEEIH RHDNVIGLRT FSKAYGLAGL RVGYAFGNAE IIAAMNKVAI
     PFAVNSAAQA AALASLNSAD ELMERVEETV EKRDAVVSAL GAAPTQANFV WLPGEGAAEL
     AAKLAEHGIV IRAFPEGARI SVTNAEETDK LLRAWEAINA G