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Entry: PATR_MYCSS
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ID   PATR_MYCSS              Reviewed;         358 AA.
AC   Q1B1Z8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   26-NOV-2014, entry version 58.
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=Mmcs_4982;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Miller C.D., Hughes J.E., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine 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; CP000384; ABG11086.1; -; Genomic_DNA.
DR   RefSeq; YP_642142.1; NC_008146.1.
DR   ProteinModelPortal; Q1B1Z8; -.
DR   STRING; 164756.Mmcs_4982; -.
DR   EnsemblBacteria; ABG11086; ABG11086; Mmcs_4982.
DR   GeneID; 4113811; -.
DR   KEGG; mmc:Mmcs_4982; -.
DR   PATRIC; 18120366; VBIMycSp106721_5097.
DR   eggNOG; COG0079; -.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; KMPVENI; -.
DR   OrthoDB; EOG6JMMWS; -.
DR   BioCyc; MSP164756:GHQ8-5040-MONOMER; -.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
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; Complete proteome; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    358       Putative phenylalanine aminotransferase.
FT                                /FTId=PRO_1000024499.
FT   MOD_RES     222    222       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01513}.
SQ   SEQUENCE   358 AA;  38892 MW;  2B0699A5838F4325 CRC64;
     MTARLRPELA DIPAYTPGKT VPGAIKIASN ETVHGPLPSV RAAIEKATDQ LNRYPDNGYL
     ELREHLASHL DKNLGAGAFT PEQIAVGCGS VSLCQQLIQI TSSVGDEVIF AWRSFEIYPL
     QVRTAGATPV QVPLRDHTHD LDAMLAAITD RTRLIFVCNP NNPTSTVVDP AALKRFVEAV
     PPHILVVIDE AYVEYIRGDQ VPDSFGLVRA HPNVVVLRTF SKAYGLAGLR IGYAVADADI
     VTALGKVYVP FSATSISQAA AIASIDAADE LLARTDQVVA ERDRVTAALR EAGFTLPPSQ
     SNFVWLPLAE RTLDFVRRAA ENRLVVRPYG EDGVRVTIAA PHENDAFLEF ARNWIGQP
//
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