ID   HIS82_PSEPF             Reviewed;         370 AA.
AC   Q3K8U2;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Histidinol-phosphate aminotransferase 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; OrderedLocusNames=Pfl01_4075;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyripides N., Anderson I., Richardson P.;
RT   "Complete sequence of Pseudomonas fluorescens PfO-1.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC       (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily.
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DR   EMBL; CP000094; ABA75812.1; -; Genomic_DNA.
DR   RefSeq; YP_349803.1; -.
DR   GeneID; 3712320; -.
DR   GenomeReviews; CP000094_GR; Pfl01_4075.
DR   KEGG; pfo:Pfl01_4075; -.
DR   HOGENOM; Q3K8U2; -.
DR   OMA; Q3K8U2; IDENTRV.
DR   BioCyc; PFLU205922:PFL_4075-MON; -.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01023; -; 1.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR005861; HisP_aminotrans.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    370       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000230221.
FT   MOD_RES     230    230       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   370 AA;  39656 MW;  C4004E8461191F0E CRC64;
     MSGNFLALAQ PGVQQLSPYV PGKPVDELAR ELDLDPASIV KLASNENPLG ASPKALAAIR
     EALDELTRYP DGNGFALKSL LAEQCRVELN QVTLGNGSND ILELVARAYL APGLNAVFSE
     HAFAVYPIAT QAVGAQAKVV PAKEWGHDLP AMLAAIDANT RVVFIANPNN PTGTWFGAEA
     LDDFLQDVPE HVLVVLDEAY IEYAEGSDLP DGLDFLAAYP NLLVSRTFSK AYGLAALRVG
     YGLSTPVVAD VLNRVRQPFN VNSLALAAAC AALKDEEYLA QSRQLNESGM QQLEAGFREL
     GLSWIPSKGN FICVDLGQVA APVFQGLLRE GVIVRPVANY GMPNHLRVTI GLPAENSRFL
     EALRKVLARG
//