ID   PATR_STRCO              Reviewed;         359 AA.
AC   Q9ZBY8;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=SCO3944; ORFNames=SCD78.11;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939118; CAA22216.1; -; Genomic_DNA.
DR   PIR; T36050; T36050.
DR   RefSeq; NP_628128.1; NC_003888.3.
DR   RefSeq; WP_011029330.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9ZBY8; -.
DR   SMR; Q9ZBY8; -.
DR   STRING; 100226.SCO3944; -.
DR   PRIDE; Q9ZBY8; -.
DR   GeneID; 1099380; -.
DR   KEGG; sco:SCO3944; -.
DR   PATRIC; fig|100226.15.peg.4016; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   InParanoid; Q9ZBY8; -.
DR   OMA; YPDMACT; -.
DR   PhylomeDB; Q9ZBY8; -.
DR   Proteomes; UP000001973; 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..359
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153521"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         223
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   359 AA;  38794 MW;  7A3C98C354E56472 CRC64;
     MSETSPKLRA ELEGIPTYKP GKPAAADGPV AYKLSSNENP YPPLPGVMET VTAAAASFNR
     YPDMACTSLM AELSDRFGVP LAHLATGTGS VGVAQQLIQA TSGPGDEVIY AWRSFEAYPI
     ITQISGARSV QVPLTPGEVH DLDAMADAIT DRTRLIFVCN PNNPTGTVVR RAELERFLDR
     VPSDVLVVLD EAYREFIRDA EVPDGVEFYR ERPNVCVLRT FSKAYGLAGL RVGFAIAHEP
     VAAALRKTAV PFGVSQIAQE AAIASLRAED ELIGRVGSLV CERARVADAL RAQGWTVPES
     QANFVWLRLG ERTLAFANAC EQAGVVVRPF AGEGVRVTVG ESEANDIFLK VSEEFRKEL