PATR_MYCVP
ID PATR_MYCVP Reviewed; 351 AA.
AC A1TGS6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Mvan_5611;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000511; ABM16376.1; -; Genomic_DNA.
DR RefSeq; WP_011782728.1; NC_008726.1.
DR AlphaFoldDB; A1TGS6; -.
DR SMR; A1TGS6; -.
DR STRING; 350058.Mvan_5611; -.
DR EnsemblBacteria; ABM16376; ABM16376; Mvan_5611.
DR KEGG; mva:Mvan_5611; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR Proteomes; UP000009159; 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 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..351
FT /note="Putative phenylalanine aminotransferase"
FT /id="PRO_1000024502"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ SEQUENCE 351 AA; 37840 MW; 8EA512952CF55A5D CRC64;
MSARLRPELA DLPAYAPGKT VPGAIKIASN ETVHGPLPSV RAAIEKAIDG INRYPDNGYV
ELRERLAKHV NFAPEYISVG CGSVSLCQQL IQITSTVGDE VLFGWRSFEI YPLQVRTAGA
TPVQVPLTDH TFDLDAMLAA ITDRTRLIFV CNPNNPTSTV VDPDALARFV EAVPPHIMVV
VDEAYVEYIR DGLAPDSFGL VRAHSNVVVL RTFSKAYGLA GLRIGYAVAD PDIIAALSKV
YVPFTATSVS QAAAIACLDA ADELLERTDA VVAERTRVSA ALREAGYDLP PSQANFVWLP
LVGRAQQFAA DAANSRVIVR PYGEDGVRVT IAAPHENDAF LGFARGWDGL R