ID   PATR_CUTAK              Reviewed;         352 AA.
AC   Q6ABU3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=PPA0034;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT81796.1; -; Genomic_DNA.
DR   RefSeq; WP_002515713.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6ABU3; -.
DR   SMR; Q6ABU3; -.
DR   STRING; 267747.PPA0034; -.
DR   EnsemblBacteria; AAT81796; AAT81796; PPA0034.
DR   KEGG; pac:PPA0034; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   Proteomes; UP000000603; 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..352
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153519"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   352 AA;  38490 MW;  3155FB18B6120851 CRC64;
     MSQDRRDVVR GLPLYKQGAS HGENAVKLSS NENPFEPLPS VVEAVTRTLP RFNRYPLMSA
     EEVRSTIAGH FGVDVSQVAV GAGSTEVASQ LMHALAGAGD EIIFPWRSFE AYPILTKVAG
     ATPIPVPLTV DLRHDLDAMA DAITDRTRVI FLCTPNNPTG TVLHTDEVVE FLARVPENVV
     VVMDEAYCHF NRDDAAVDGL TLLEDHPNVV VLRTFSKAYG LAGLRIGFAI STPEISDDLR
     RVATPFTVTT LAQQAAIASL AAEDELNERV NRIVAERTRV FDELTRQGWK IVPSQANFLW
     LATGDDTDRI DEVMVSHGVF ARCWSEEGIR LSIGLDAEND RAIEALSQAV KG