ID   HIS81_PSYA2             Reviewed;         380 AA.
AC   Q4FSH2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Psyc_1185;
OS   Psychrobacter arcticus (strain DSM 17307 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   NASA Astrobiology Institute;
RA   Ayala-del-Rio H.L., Chain P., Ponder M.A., Di Bartolo G., Ivanova N.,
RA   Bergholz P.W., Hauser L., Land M., Bakermans C., Rodrigues D.,
RA   Klappenbach J.A., Zarka D., Larimer F., Richardson P., Thomashow M.F.,
RA   Tiedje J.M.;
RT   "Complete sequence of Psychrobacter arcticum 273-4.";
RL   Submitted (JUL-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; CP000082; AAZ19036.1; -; Genomic_DNA.
DR   RefSeq; YP_264470.1; -.
DR   GeneID; 3514083; -.
DR   GenomeReviews; CP000082_GR; Psyc_1185.
DR   KEGG; par:Psyc_1185; -.
DR   NMPDR; fig|259536.4.peg.788; -.
DR   HOGENOM; Q4FSH2; -.
DR   OMA; Q4FSH2; KGYIVRS.
DR   BioCyc; PARC259536:PSYC_1185-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    380       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000153426.
FT   MOD_RES     235    235       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   380 AA;  41809 MW;  E2B3C8656D940EA6 CRC64;
     MQSTQSTESN LLPLVPAYDS ILALAPYQTG KPIEELTREY GVSDVVKLAS NENPIGCSPH
     VTLAITEQIG QLSRYPDGNG YYLKQALADF NDVNVDQITL GNGSDDLLDI LARSFVGADD
     AIVYSQYAFV VYSMLAKMQG AMDVEVPAQR FGHDLKAMSQ AIENNSNTKI VFIANPNNPT
     GTQLEHGELR EFVASVPSSV LVVLDEAYIE YSPESNNRAL LDEFDNVVIV RTFSKAYGLA
     GLRVGYALSS AAVADLLNRI RQPFNVSRVA LAAAAAALAD QDFIEKTRLI NDEQMHWLEK
     QFDALGLGFI KSHANFIMVE IAVEMEDTNA AVIYQALLEQ GVIVRQLEVY GLYNWLRISV
     GVAEDNMRLI DTLRSILTDD
//