ID   PATR_MYCS2              Reviewed;         361 AA.
AC   A0R5X8; I7GAM4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
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};
GN   OrderedLocusNames=MSMEG_6351, MSMEI_6185;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK70318.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42612.1; -; Genomic_DNA.
DR   RefSeq; WP_011731224.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890566.1; NC_008596.1.
DR   AlphaFoldDB; A0R5X8; -.
DR   SMR; A0R5X8; -.
DR   STRING; 246196.MSMEI_6185; -.
DR   EnsemblBacteria; ABK70318; ABK70318; MSMEG_6351.
DR   EnsemblBacteria; AFP42612; AFP42612; MSMEI_6185.
DR   GeneID; 66737631; -.
DR   KEGG; msg:MSMEI_6185; -.
DR   KEGG; msm:MSMEG_6351; -.
DR   PATRIC; fig|246196.19.peg.6182; -.
DR   eggNOG; COG0079; Bacteria.
DR   OMA; YPDMACT; -.
DR   OrthoDB; 1248286at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..361
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_1000024496"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   361 AA;  38871 MW;  1E1851D681D311E4 CRC64;
     MSIRLRAEMA DLPAYAPGKT VPGAIKIASN ETVHGPLPSV REAILKATDL INRYPDNGYL
     DLRERLAKHV NFAPENISVG CGSVSLCQQL IQITSSVGDE VLFAWRSFEI YPLQVRTAGA
     TPVAVALRDH THDLDAMLAA ITDRTRLIFV CNPNNPTSTV VDPGELARFV AAVPPHILVV
     LDEAYVEYIR DGLLPDSLGL VREHRNVVVL RTFSKAYGLA GLRVGYAVAD PEIVTALGKV
     YVPFSATSVS QAAAIACLDA ADELLARTDA VVAERTRVSD ALRAAGYTLP PSQANFVWLP
     LAERTLDFVA RAADNRIIVR PYGEDGVRVT IGAPHENDAF LDFAQRWIAP GGAGPRTGDS
     A