ID   PATR_MYCTO              Reviewed;         353 AA.
AC   P9WML4; L0TGI3; P72039;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
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=MT3881;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK48246.1; -; Genomic_DNA.
DR   PIR; H70694; H70694.
DR   RefSeq; WP_003899686.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WML4; -.
DR   SMR; P9WML4; -.
DR   EnsemblBacteria; AAK48246; AAK48246; MT3881.
DR   KEGG; mtc:MT3881; -.
DR   PATRIC; fig|83331.31.peg.4176; -.
DR   HOGENOM; CLU_017584_3_3_11; -.
DR   Proteomes; UP000001020; 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_0000427283"
FT   MOD_RES         217
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
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