ID   HIS82_DECAR             Reviewed;         356 AA.
AC   Q47AL9;
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 2;
DE            EC=2.6.1.9;
DE   AltName: Full=Imidazole acetol-phosphate transaminase 2;
GN   Name=hisC2; OrderedLocusNames=Daro_3383;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Dechloromonas.
OX   NCBI_TaxID=159087;
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., Di Bartolo G., Trong S., Kellar K.,
RA   Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT   "Complete sequence of Dechloromonas aromatica RCB.";
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; CP000089; AAZ48112.1; -; Genomic_DNA.
DR   RefSeq; YP_286582.1; -.
DR   GeneID; 3567113; -.
DR   GenomeReviews; CP000089_GR; Daro_3383.
DR   KEGG; dar:Daro_3383; -.
DR   NMPDR; fig|159087.4.peg.3631; -.
DR   HOGENOM; Q47AL9; -.
DR   OMA; Q47AL9; AAYEDDA.
DR   BioCyc; DARO159087:DARO_3383-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    356       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153353.
FT   MOD_RES     214    214       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   356 AA;  39296 MW;  B54E4A301D925E92 CRC64;
     MSRFWSQVVR DLTPYVPGEQ PKIANLIKLN TNENPFPPSP RVVAAIQAEL GDDAARLRLY
     PDPNADLLKA AVARRHTVSA QQVFVGNGSD EVLAHIFMAL LKHDQPIIFP DITYSFYPVY
     CGLYGVEYQT LPLADDFSIN PADYCDRPNG GIIFPNPNAP TGRLLPLDAI EQMLKANPDS
     VVVVDEAYVD FGGETAISLV DRYDNLLVVH TLSKSRSLAG MRVGFAVGHA ALIEALERVK
     NSFNSYPLDR LAIVAAVAAM EDEAYFAQCC HAVMATRNTL TAELTELGFE VLPSTANFIF
     TRHPQRDAAE LAKALRERNI IVRHFKLPRI DQFLRITVGT DGECKALTDA LRQITG
//