ID   PATR_MYCPA              Reviewed;         355 AA.
AC   P61005;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
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}; Synonyms=hisC2;
GN   OrderedLocusNames=MAP_0252c;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02569.1; -; Genomic_DNA.
DR   RefSeq; WP_010948792.1; NC_002944.2.
DR   AlphaFoldDB; P61005; -.
DR   SMR; P61005; -.
DR   STRING; 262316.MAP_0252c; -.
DR   EnsemblBacteria; AAS02569; AAS02569; MAP_0252c.
DR   KEGG; mpa:MAP_0252c; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   OMA; YPDMACT; -.
DR   Proteomes; UP000000580; 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..355
FT                   /note="Putative phenylalanine aminotransferase"
FT                   /id="PRO_0000153516"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ   SEQUENCE   355 AA;  37975 MW;  99CDA281C3CF8E41 CRC64;
     MTARLRPELA GLPVYVPGKN VPGSIKLASN ETVYGPLPSV HAAIERAVAV VNRYPDNACV
     DLKAALAMHL GSDVAPEQIA VGSGSVTLCQ QLVQITSAAG DEVMMGWRSF ECYLPIVQVA
     GAIAVKVPLR EHTYDLDAML AAITDRTRLI FVCNPNNPTS TVVDPDALVR FVDAVPADIL
     IAIDEAYVEY IRDGLLPNSL ELALSRSNVV VLRTFSKAYG LAGLRVGYAI GHPELITALD
     KVVMPFAVTN VAQAAAIASL EASGELMART DALVAERTRV STALRDAGFE LPPSQANFLW
     LPLGSRTEDF VQEAANARLV VRPFASEGVR VTIGAPAEND ALLQFACDWI ARTER