ID   HIS81_PSEPF             Reviewed;         350 AA.
AC   Q3KHZ1;
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 1;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN   Name=hisC1; OrderedLocusNames=Pfl01_0872;
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; ABA72615.1; -; Genomic_DNA.
DR   RefSeq; YP_346604.1; -.
DR   GeneID; 3715605; -.
DR   GenomeReviews; CP000094_GR; Pfl01_0872.
DR   KEGG; pfo:Pfl01_0872; -.
DR   HOGENOM; Q3KHZ1; -.
DR   OMA; Q3KHZ1; DEQFQIR.
DR   BioCyc; PFLU205922:PFL_0872-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    350       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000230220.
FT   MOD_RES     210    210       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   350 AA;  38555 MW;  88FCD2975D58367C CRC64;
     MSKFWSPFVK DLVPYVPGEQ PKLTRLVKLN TNENPYGPSP KALAAMQAEL NDNLRLYPDP
     NSDLLKNAVA KYYGVQNNQV FLGNGSDEVL AHIFHGLLQH DQPILFPDIS YSFYPVYCGL
     YGITFDAVPL DAQFRINPAD YAKPNGGIIF PNPNAPTGCL LALEAVEQIL KGSPDSVVVV
     DEAYIDFGGE TAISLVDRYP NLLVTQTLSK SRSLAGLRVG LAVGHPDLIE ALERIKNSFN
     SYPIDRMANV GAAAAFEDRE YFDKTCALVI ESREWVVAQL QAKGFEVLPS AANFIFARHP
     QHDAAGLAAK LREQGVIVRH FKQERIAQFL RISIGTPEQN QALIDGLGEL
//