ID HIS7_HAEI8 Reviewed; 362 AA. AC Q4QN72; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 24. DE RecName: Full=Histidine biosynthesis bifunctional protein hisB; DE Includes: DE RecName: Full=Histidinol-phosphatase; DE EC=3.1.3.15; DE Includes: DE RecName: Full=Imidazoleglycerol-phosphate dehydratase; DE Short=IGPD; DE EC=4.2.1.19; GN Name=hisB; OrderedLocusNames=NTHI0602; 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: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol CC + phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: In the N-terminal section; belongs to the histidinol- CC phosphatase family. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC imidazoleglycerol-phosphate dehydratase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000057; AAX87525.1; -; Genomic_DNA. DR RefSeq; YP_248185.1; -. DR GeneID; 3429912; -. DR GenomeReviews; CP000057_GR; NTHI0602. DR KEGG; hit:NTHI0602; -. DR HOGENOM; Q4QN72; -. DR OMA; Q4QN72; MVSNQDG. DR BioCyc; HINF281310:NTHI0602-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:HAMAP. DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase act...; IEA:HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_01022; -; 1. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR InterPro; IPR005954; HisB_N. DR InterPro; IPR006543; Histidinol-phos. DR InterPro; IPR000807; Imidazole_glycer-P_deHydtase. DR InterPro; IPR013954; PNK3P_central-region. DR PANTHER; PTHR23133:SF2; Imidazole-GPD; 1. DR Pfam; PF00475; IGPD; 1. DR Pfam; PF08645; PNK3P; 1. DR ProDom; PD002282; IGPD; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. DR TIGRFAMs; TIGR01261; hisB_Nterm; 1. DR TIGRFAMs; TIGR01656; Histidinol-ppas; 1. DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1. DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Lyase; Multifunctional enzyme. FT CHAIN 1 362 Histidine biosynthesis bifunctional FT protein hisB. FT /FTId=PRO_1000063445. FT REGION 1 173 Histidinol-phosphatase. FT REGION 174 362 Imidazoleglycerol-phosphate dehydratase. SQ SEQUENCE 362 AA; 41189 MW; D4628788FF37B586 CRC64; MQPTLFIDRD GTLIDEPKTD FQIDSLEKLK LEPKVIPALL RLKAKYRFVI VSNQDGLGTD AFPQTNFDKP HNVMMALFES QGITFDEVLI CPHKPEENCL CRKPKIKLLD HYIRKNLFDI DRSFVIGDRE TDVQLAENLG IRAIQYDPQK MNWDLIAEKL LGETVTNCGK RPPRFAEVIR QTKETDIKVQ IWLDEAGVNE IKTGVGFFDH MLDQIATHGG FRMNVQCKGD LWIDEHHTVE DTALALGQAL KQAIGDKRGI ARFGFVLPMD ECKAECALDL SGRPWIKFNA CFKRDKVGDF STELTEHFFQ SLAFSMLATI HLNVTGNNDH HKIESLFKAF GRTLRQAIRI EGNEMPSSKG VL //