PATR_MYCBP
ID PATR_MYCBP Reviewed; 353 AA.
AC A1KQA5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=BCG_3833;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL73823.1; -; Genomic_DNA.
DR RefSeq; WP_003420576.1; NC_008769.1.
DR AlphaFoldDB; A1KQA5; -.
DR SMR; A1KQA5; -.
DR KEGG; mbb:BCG_3833; -.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OMA; YPDMACT; -.
DR Proteomes; UP000001472; 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 PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Transferase.
FT CHAIN 1..353
FT /note="Putative phenylalanine aminotransferase"
FT /id="PRO_1000024495"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ SEQUENCE 353 AA; 38009 MW; ED5BBE2AD2DFC25F CRC64;
MTARLRPELA GLPVYVPGKT VPGAIKLASN ETVFGPLPSV RAAIDRATDT VNRYPDNGCV
QLKAALARHL GPDFAPEHVA VGCGSVSLCQ QLVQVTASVG DEVVFGWRSF ELYPPQVRVA
GAIPIQVPLT DHTFDLYAML AAVTDRTRLI FVCNPNNPTS TVVGPDALAR FVEAVPAHIL
IAIDEAYVEY IRDGMRPDSL GLVRAHNNVV VLRTFSKAYG LAGLRIGYAI GHPDVITALD
KVYVPFTVSS IGQAAAIASL DAADELLART DTVVAERARV SAELRAAGFT LPPSQANFVW
LPLGSRTQDF VEQAADARIV VRPYGTDGVR VTVAAPEEND AFLRFARRWR SDQ