PATR_MYCA1
ID PATR_MYCA1 Reviewed; 355 AA.
AC A0Q9F3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=MAV_0250;
OS Mycobacterium avium (strain 104).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=243243;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-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; CP000479; ABK66277.1; -; Genomic_DNA.
DR RefSeq; WP_009974504.1; NC_008595.1.
DR AlphaFoldDB; A0Q9F3; -.
DR SMR; A0Q9F3; -.
DR EnsemblBacteria; ABK66277; ABK66277; MAV_0250.
DR KEGG; mav:MAV_0250; -.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR Proteomes; UP000001574; 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; Transferase.
FT CHAIN 1..355
FT /note="Putative phenylalanine aminotransferase"
FT /id="PRO_1000024494"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ SEQUENCE 355 AA; 38019 MW; 7444BA6C61940A2C CRC64;
MTARLRPELA GLPVYVPGKN VPGSIKLASN ETVYGPLPSV HAAIERAVAI VNRYPDNACV
DLKAALAMHL GSDVAPEQIA VGSGSVTLCQ QLVQITSAAG DEVMMGWRSF ECYLPIVQVA
GAIAVKVPLR EHTYDLDAML AAITDRTRLI FVCNPNNPTS TVVDPDALVR FVDAVPADIL
IAIDEAYVEY IRDGLLPNSL ELALSRSNVV VLRTFSKAYG LAGLRVGYAI GHPELITALD
KVVMPFAVTN VAQAAAIASL EASGELMART DALVAERTRV STTLRDAGFE LPPSQANFLW
LPLGSRTEDF VQEAANARLV VRPFASEGVR VTIGAPAEND ALLQFACDWI ARTER