ID   PATR_RHOOB              Reviewed;         358 AA.
AC   C1B997;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=ROP_40030;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; AP011115; BAH52250.1; -; Genomic_DNA.
DR   RefSeq; WP_012691187.1; NC_012522.1.
DR   AlphaFoldDB; C1B997; -.
DR   SMR; C1B997; -.
DR   STRING; 632772.ROP_40030; -.
DR   EnsemblBacteria; BAH52250; BAH52250; ROP_40030.
DR   KEGG; rop:ROP_40030; -.
DR   PATRIC; fig|632772.20.peg.4199; -.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   Proteomes; UP000002212; 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; Transferase.
FT   CHAIN           1..358
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_1000185065"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   358 AA;  37535 MW;  7AD4019A5ABE3505 CRC64;
     MTPRTRTDLD TITAYVPGKS YPGAIKLASN ETTLGPLPSV RDAIADAAAN ANRYPDNGHV
     ALIAAIADHF GVATANVAVG AGSVSLCQEL VHATCNDGDE VMFAWRSFEA YPVVTRVAGA
     VPVTVPLTAD YRHDLDAMAA AVTDRTRLIF VCTPNNPTGP ALSTSELERF LDAVPDRVVV
     ALDEAYFEYN RSGTDGLDLF RRYPNVVVLR TFSKAYGLAG LRVGYAIADA AIVAALSKVH
     IAFTVNAVAQ AAAIASLAAS GELLARTDGV VAERNRVRDA LLAAGYEVPE SDANFVYLPL
     GSRSGAFGAA SAEAGVLLRP YGDDGVRITI GDPEENDAFL AFATSTEARS IANVAVRA