ID   HIS81_RALEJ             Reviewed;         376 AA.
AC   Q46Y48;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-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=Reut_A2574;
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; AAZ61935.1; -; Genomic_DNA.
DR   RefSeq; YP_296779.1; -.
DR   GeneID; 3609598; -.
DR   GenomeReviews; CP000090_GR; Reut_A2574.
DR   KEGG; reu:Reut_A2574; -.
DR   NMPDR; fig|264198.3.peg.3328; -.
DR   HOGENOM; Q46Y48; -.
DR   OMA; Q46Y48; PLGMPKS.
DR   BioCyc; REUT264198:REUT_A2574-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    376       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000153428.
FT   MOD_RES     235    235       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   376 AA;  40148 MW;  0BBC3BE84C51C3BD CRC64;
     MAEQGKQGGK VPFGPDYVRA ISPYIAGKPI SEVAREFGLD EAGIVKLASN ENPLGMPESA
     KHAAAAAIAE LGRYPDSNGF ELKAALSTKL GVPQDWLTLG NGSNDILELA AHALVTPGQS
     IVYAEYSFAV YALATQEIGA RAIVVKARDY GHDLDAMAAA ITSDTRLVFI ANPNNPTGTF
     VPAAALETFL AKVPAEVVVV LDEAYNEYLD DDQQYDSVAW VRRYPNLLVS RTFSKAYGLA
     GLRIGYAVAQ PELTDLLNRI RQPFNVNSVA QAAAVAALGD TAFLQRSAEL NRAGKAQLVE
     AFSRLGLEFV ASSGNFVLVR VGDDDDAGAR VNVALLRQGV IVRPVGNYGM PRWLRVTIGL
     PDENAAFIAA LERALK
//