ID   HIS82_RALEJ             Reviewed;         366 AA.
AC   Q46WL3;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=Reut_A3110;
OS   Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
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., Goltsman E., Martinez M.,
RA   Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Ralstonia eutropha JMP134.";
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; CP000090; AAZ62470.1; -; Genomic_DNA.
DR   RefSeq; YP_297314.1; -.
DR   PDB; 3EUC; X-ray; 2.05 A; A/B=1-366.
DR   PDBsum; 3EUC; -.
DR   GeneID; 3609701; -.
DR   GenomeReviews; CP000090_GR; Reut_A3110.
DR   KEGG; reu:Reut_A3110; -.
DR   NMPDR; fig|264198.3.peg.3550; -.
DR   HOGENOM; Q46WL3; -.
DR   OMA; Q46WL3; RIQTIEH.
DR   BioCyc; REUT264198:REUT_A3110-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; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW   Complete proteome; Histidine biosynthesis; Pyridoxal phosphate;
KW   Transferase.
FT   CHAIN         1    366       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153429.
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   366 AA;  39607 MW;  D979A3B063F852E6 CRC64;
     MSVVDPSLIE RIIRDDVRAM GAYHVPDSHG LVKLDAMENP YRLPPALRSE LAARLGEVAL
     NRYPVPSSEA LRAKLKEVMQ VPAGMEVLLG NGSDEIISML ALAAARPGAK VMAPVPGFVM
     YAMSAQFAGL EFVGVPLRAD FTLDRGAMLA AMAEHQPAIV YLAYPNNPTG NLFDAADMEA
     IVRAAQGSVC RSLVVVDEAY QPFAQESWMS RLTDFGNLLV MRTVSKLGLA GIRLGYVAGD
     PQWLEQLDKV RPPYNVNVLT EATALFALEH VAVLDEQAAQ LRAERSRVAE GMAAHGGVTV
     FPSAANFLLA RVPDAAQTFD RLLARKVLIK NVSKMHPLLA NCLRVTVSTP EENAQFLEAF
     AASLQD
//