ID   HIS81_DECAR             Reviewed;         362 AA.
AC   Q47GP2;
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=Daro_1233;
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; AAZ45989.1; -; Genomic_DNA.
DR   RefSeq; YP_284459.1; -.
DR   GeneID; 3569417; -.
DR   GenomeReviews; CP000089_GR; Daro_1233.
DR   KEGG; dar:Daro_1233; -.
DR   NMPDR; fig|159087.4.peg.932; -.
DR   HOGENOM; Q47GP2; -.
DR   OMA; Q47GP2; PLGMPKS.
DR   BioCyc; DARO159087:DARO_1233-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    362       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000153352.
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   362 AA;  39502 MW;  CF3EBA40D23D7D31 CRC64;
     MSLADQALSY VRAISPYQPG KPITELAREM GIPVEKIVKL ASNENPLGMS PKARKAVEAA
     ISGIERYPDQ FDLIAKVAER CGVSSNQIVL GNGSNDVLDL IARVFLAPGR SAVFAQHAFA
     VYPLATLSTG AELISTPAKN YGHDLNAMRA AIRPDTRIVW IANPNNPTGN FLPYPEVRAF
     LEVVPKDVVV VLDEAYNEYI PPAERVDTAT WIKDFPNLVV CRTFSKIFGL AGLRVGYALA
     STEVADLMNR IRQPFNVNNL AIAAAVAALD DHLFVADSYE LNRRGMEQII AGLKRFGLEH
     IPSHGNFVTF RAGDAAVVNQ KLLKQGVIVR PIGGYGLPEW LRVTIGTEPE NARFLEALEK
     AL
//