PATR_CORDI
ID PATR_CORDI Reviewed; 344 AA.
AC P61004;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=DIP0178;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(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}.
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DR EMBL; BX248354; CAE48682.1; -; Genomic_DNA.
DR RefSeq; WP_010934082.1; NC_002935.2.
DR AlphaFoldDB; P61004; -.
DR SMR; P61004; -.
DR STRING; 257309.DIP0178; -.
DR EnsemblBacteria; CAE48682; CAE48682; DIP0178.
DR KEGG; cdi:DIP0178; -.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR Proteomes; UP000002198; 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..344
FT /note="Putative phenylalanine aminotransferase"
FT /id="PRO_0000153510"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ SEQUENCE 344 AA; 37000 MW; 97057C59E9FEB49D CRC64;
MIRKDLSQIP TYVPGKRNDH ALKLSSNEVT HRPLPSAAQA MAEAAAGANR YPDMGVTELR
GALSEHLGVP AEQIAVGCGS SALCQQLVQI TCTPGDEVVF PWRSFEAYPI FVQVVGATPV
AVPLTSDGFN DLDAMAAAIT PKTKLVFVCN PNNPSGTVVR REAFLEFMAK VPADVVVALD
EAYTEYVRDE DTIFATEILS EFPNLVGLRT FSKAFGLAGV RVGYAFGPHE LIDALNKVAL
PFGVNAVGQA GALASLNNLD ELMEHTEEVV AVRDRVADHI GAAHSQANFV WIPAESRSET
PFEIAEKLAA HDVLVRAFPE GVRITVTNEE ESDRLLAAWD ASFA