ID   HIS81_HAEI8             Reviewed;         352 AA.
AC   Q4QN73;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   26-MAY-2009, entry version 24.
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=NTHI0601;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87524.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_248184.1; -.
DR   GeneID; 3429911; -.
DR   GenomeReviews; CP000057_GR; NTHI0601.
DR   KEGG; hit:NTHI0601; -.
DR   HOGENOM; Q4QN73; -.
DR   BioCyc; HINF281310:NTHI0601-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    352       Histidinol-phosphate aminotransferase 1.
FT                                /FTId=PRO_0000153370.
FT   MOD_RES     211    211       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   352 AA;  38891 MW;  FFACC8DB2C4A15C9 CRC64;
     MTITTLSRQN IQALTPYQSA RKLGGNGTIW LNANEYPTSP EFQLSGKDLN RYPEPQPQRV
     VQAYANYAGV STENVLVTRG GDEGIELIIH TFCEPKQDAI LFCPPTYGMY AVSAETAGVL
     SKSVPLTDDF QLNLPEIKNH LNDVKVVFVC SPNNPTGNLL KQSDILDLLQ ITAGKAIVVV
     DEAYIEFCPE ASVINLLKNY PHLAIIRTLS KAFALAGLRC GFVLANPELI DILSKVIAPY
     PIPVPSADLA EQALRPANIA TVQALTQELL SNRQWLAKAL LVLHQVEKVY ESEANYLLIK
     CQNGQAVFKA LWEQGIILRD QNKTLHLQNC IRITVGTRNE CEKVVEAIKE VK
//