ID A5WTZ2_MYCTF Unreviewed; 353 AA.
AC A5WTZ2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 01-MAY-2013, entry version 29.
DE RecName: Full=Putative phenylalanine aminotransferase;
DE EC=2.6.1.-;
GN Name=pat; OrderedLocusNames=TBFG_13806;
OS Mycobacterium tuberculosis (strain F11).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC Mycobacterium tuberculosis complex.
OX NCBI_TaxID=336982;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Grabherr M., Mauceli E., Brockman W., Young S., LaButti K.,
RA Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T.,
RA Zimmer A., Settipalli S., Shea T., Arachchi H., Macdonald P.,
RA Abouelleil A., Lui A., Priest M., Berlin A., Gearin G., Brown A.,
RA Aftuck L., Bessette D., Allen N., Lubonja R., Lokyitsang T.,
RA Matthews C., Dunbar C., Benamara M., Nguyen T., Negash T.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA Alvarado L., Victor T., Murray M.;
RT "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL Submitted (APR-2007) 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000717; ABR08131.1; -; Genomic_DNA.
DR RefSeq; YP_001289733.1; NC_009565.1.
DR ProteinModelPortal; A5WTZ2; -.
DR SMR; A5WTZ2; 5-346.
DR STRING; 336982.TBFG_13806; -.
DR EnsemblBacteria; ABR08131; ABR08131; TBFG_13806.
DR GeneID; 5224501; -.
DR KEGG; mtf:TBFG_13806; -.
DR PATRIC; 18139199; VBIMycTub9078_4225.
DR eggNOG; COG0079; -.
DR HOGENOM; HOG000288510; -.
DR KO; K00817; -.
DR OMA; NNTKIVW; -.
DR ProtClustDB; PRK03321; -.
DR BioCyc; MTUB336982:GH7I-3845-MONOMER; -.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:InterPro.
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; IPR024892; AroT.
DR InterPro; IPR005861; HisP_aminotrans.
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 PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
FT MOD_RES 217 217 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 353 AA; 38040 MW; E5E49F74DC2436F4 CRC64;
MTARLRPELA GLPVYVPGKT VPGAIKLASN ETVFGPLPSV RAAIDRATDT VNRYPDNGCV
QLKAALARHL GPDFAPEHVA VGCGSVSLCQ QLVQVTASVG DEVVFGWRSF ELYPPQVRVA
GAIPIQVPLT DHTFDLYAML ATVTDRTRLI FVCNPNNPTS TVVGPDALAR FVEAVPAHIL
IAIDEAYVEY IRDGMRPDSL GLVRAHNNVV VLRTFSKAYG LAGLRIGYAI GHPDVITALD
KVYVPFTVSS IGQAAAIASL DAADELLART DTVVAERARV SAELRAAGFT LPPSQANFVW
LPLGSRTQDF VEQAADARIV VRPYGTDGVR VTVAAPEEND AFLRFARRWR SDQ
//
