ID   HIS81_PSEF5             Reviewed;         350 AA.
AC   Q4KI72;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=PFL_0930;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY90217.1; -; Genomic_DNA.
DR   RefSeq; YP_258061.1; -.
DR   GeneID; 3475458; -.
DR   GenomeReviews; CP000076_GR; PFL_0930.
DR   KEGG; pfl:PFL_0930; -.
DR   NMPDR; fig|220664.3.peg.2374; -.
DR   HOGENOM; Q4KI72; -.
DR   OMA; Q4KI72; DEQFQIR.
DR   BioCyc; PFLU220664:PFL_0930-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_0000153419.
FT   MOD_RES     210    210       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   350 AA;  38647 MW;  03DB8954A241DB2D CRC64;
     MSKFWSPFVK NLVPYVPGEQ PKLTKLVKLN TNENPYGPSP RALAAMQAEL NDNLRLYPDP
     NSDLLKQAVA SYYGVQGNQV FLGNGSDEVL AHIFHGLLQQ EKPLLFPDIS YSFYPVYCGL
     YGIEHEAVPL DEQFQIRVAD YARPNGGIIF PNPNAPTGCL LALDAVEQIL KASPDSVVVV
     DEAYIDFGGQ TAISLVDRYP NLLVTQTLSK SRSLAGLRVG LAVGHPDLIE ALERVKNSFN
     SYPLDRLAIV GAAAAFEDRE YFAKTCQQVI DSREWVVAQL QAKGFEVLPS AANFIFARHP
     RHDAAGLAAK LREQGVIVRH FKQQRIAQFL RISIGTQEQN QALIDGLGEL
//