ID   PATR_RHOE4              Reviewed;         358 AA.
AC   C0ZM44;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=RER_03130;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC   Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
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-2005) 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; AP008957; BAH31021.1; -; Genomic_DNA.
DR   RefSeq; WP_020905850.1; NC_012490.1.
DR   AlphaFoldDB; C0ZM44; -.
DR   SMR; C0ZM44; -.
DR   STRING; 234621.RER_03130; -.
DR   EnsemblBacteria; BAH31021; BAH31021; RER_03130.
DR   KEGG; rer:RER_03130; -.
DR   PATRIC; fig|234621.6.peg.748; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   Proteomes; UP000002204; 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_1000215348"
FT   MOD_RES         214
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   358 AA;  37671 MW;  524249B8B83F6140 CRC64;
     MTAHIRPDLA SIPAYVPGRN FPGAIKLASN ETTVGPLPGV RDAVADAVAN ANRYPDNAAV
     ALIEALASFL KVEPANVAAG CGSVTLCQEL VQITCDQGDE VIYAWRSFEA YPVVTQVGHA
     VSVKVPLTED FGHDLDAMLA AITDRTRLIF VCNPNNPTGN ALSKAELESF LDAVPAHVVV
     ALDEAYFEYS RSDADGIELF RSRPNVVVLR TFSKAYGLAG IRVGYAVADP EIIVALGKVH
     TPFTVSAVAQ AAAIASLAAA DELLARTEGV IAERTRVRTA LIEAGYTVPE SSANFVYLPL
     GELSPAFAEA STEAGILIRQ YGVEGVRMTI GDPHENDAFL AFADTDVAKQ AAGIGVSA