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 29-MAY-2013, entry version 52.
DE RecName: Full=Putative phenylalanine aminotransferase;
DE EC=2.6.1.-;
GN Name=pat; 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 (By similarity).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family.
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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; NNTKIVW; -.
DR ProtClustDB; PRK03321; -.
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_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; PyrdxlP-dep_Trfase_major; 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 (By
FT similarity).
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
//
