ID   HIS82_THIDA             Reviewed;         357 AA.
AC   Q3SI68;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Tbd_1712;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Hydrogenophilales;
OC   Hydrogenophilaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16452431; DOI=10.1128/JB.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic,
RT   facultatively anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97665.1; -; Genomic_DNA.
DR   RefSeq; YP_315470.1; -.
DR   GeneID; 3671295; -.
DR   GenomeReviews; CP000116_GR; Tbd_1712.
DR   KEGG; tbd:Tbd_1712; -.
DR   NMPDR; fig|292415.3.peg.1809; -.
DR   HOGENOM; Q3SI68; -.
DR   OMA; Q3SI68; DEQFQIR.
DR   BioCyc; TDEN292415:TBD_1712-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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    357       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153472.
FT   MOD_RES     215    215       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   357 AA;  38963 MW;  2B183CEAFDE2C561 CRC64;
     MSRTSTSRYW SAVVGALTPY VPGEQPKLAN LVKLNTNENP YGPSPRVLEA LRGEVGDTLR
     LYPDPNSDRL RAAIAAYHAV SPDQVFVGNG SDEVLAHTFL ALLKHERPVF FPDITYSFYP
     VYCGLYGIAH RAIPLDDAFE IRVDDYLAPK GGVIFPNPNA PTGRLLALGE IERLLAANRD
     SVVVIDEAYV DFGGDSAVPL VARHPQLLVT RTLSKSHALA GLRVGYAVGQ APLIEALNRV
     KDSFNSYPLD RFAQAGALAS IEDRAYFESI CARVIATRTR LVDAMESLGF EVLPSAANFI
     FARHPAHDGE ALAARLRERS IIVRHFKNPA RIAPFLRITV GTDAQCDALV DALKALC
//