ID   HIS82_HAEI8             Reviewed;         366 AA.
AC   Q4QLD1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-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=NTHI1334;
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; AAX88166.1; -; Genomic_DNA.
DR   RefSeq; YP_248826.1; -.
DR   GeneID; 3430594; -.
DR   GenomeReviews; CP000057_GR; NTHI1334.
DR   KEGG; hit:NTHI1334; -.
DR   HOGENOM; Q4QLD1; -.
DR   OMA; Q4QLD1; KGYIVRS.
DR   BioCyc; HINF281310:NTHI1334-MON; -.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IEA:InterPro.
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; IPR001176; ACC_synthase.
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   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
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    366       Histidinol-phosphate aminotransferase 2.
FT                                /FTId=PRO_0000153371.
FT   MOD_RES     226    226       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   366 AA;  41035 MW;  F8111B502A86EE29 CRC64;
     MQYINIANRG VKSLSPYQAG KPIEELEREI GISNIVKLAS NENPFGFPES AKKAIFEQLD
     KLTRYPDANG FELKQTIAKK FGVQPNQITL GNGSNDLLEL FAHTFATEGD EIIYSQYAFI
     VYPLVTKAIN AIAKEIPAKN WGHDLQGFLT ALSDKTKLIY IANPNNPTGN FLTSQEIEDF
     LAKVPENVIV VLDEAYTEFT RSEERVDSFS LLKKYSNLII SRTLSKAYGL AGLRIGYAVS
     NPEIADLLNR VRQPFNCNSL ALTAAVAVMN DDEFIEKVAE NNRIEMRRYE DFCQKNQLDY
     IPSKGNFITI DFKQPAAPIY DALLREGVIV RPIAGYGMPN HLRISIGLPE ENDKFFTALS
     KVLKFA
//