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Database: UniProt
Entry: A5UGY3
LinkDB: A5UGY3
Original site: A5UGY3 
ID   HIS7_HAEIG              Reviewed;         362 AA.
AC   A5UGY3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   29-OCT-2014, entry version 53.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022};
GN   OrderedLocusNames=CGSHiGG_05600;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R.,
RA   Post J.C., Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12
RT   clinical nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3-
CC       phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol
CC       + phosphate. {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01022}.
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DR   EMBL; CP000672; ABR00039.1; -; Genomic_DNA.
DR   RefSeq; WP_011961666.1; NC_009567.1.
DR   RefSeq; YP_001292422.1; NC_009567.1.
DR   ProteinModelPortal; A5UGY3; -.
DR   STRING; 374931.CGSHiGG_05600; -.
DR   EnsemblBacteria; ABR00039; ABR00039; CGSHiGG_05600.
DR   GeneID; 5226441; -.
DR   KEGG; hiq:CGSHiGG_05600; -.
DR   PATRIC; 20186492; VBIHaeInf102487_1127.
DR   eggNOG; COG0131; -.
DR   HOGENOM; HOG000228065; -.
DR   KO; K01089; -.
DR   OMA; GTDSFPQ; -.
DR   OrthoDB; EOG60PHGP; -.
DR   BioCyc; HINF374931:GJA4-966-MONOMER; -.
DR   UniPathway; UPA00031; UER00011.
DR   UniPathway; UPA00031; UER00013.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   HAMAP; MF_01022; Bifunc_HisB; 1.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR020566; His_synth_bifunc_HisB.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   PANTHER; PTHR23133:SF2; PTHR23133:SF2; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF54211; SSF54211; 2.
DR   SUPFAM; SSF56784; SSF56784; 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_1000063447.
FT   REGION        1    173       Histidinol-phosphatase.
FT   REGION      174    362       Imidazoleglycerol-phosphate dehydratase.
SQ   SEQUENCE   362 AA;  41207 MW;  F9D83E2441C375C9 CRC64;
     MQPTLFIDRD GTLIDEPKTD FQIDSLEKLK LEPKVIPALL RLKAKYRFVI VSNQDGLGTD
     AFPQTNFDKP HNVMMALFES QGITFDEVLI CPHKPEENCL CRKPKIKLLD HYIRKNLFDI
     DRSFVIGDRE TDMQLAENLG IRAIQYDPQK MNWDLIAEKL LGETVTNCGK RPPRFAEVIR
     QTKETDIKVQ VWLDEAGVNE IKTGVGFFDH MLDQIATHGG FRMNVQCKGD LWIDEHHTVE
     DTALALGQAL KQAIGDKRGI ARFGFVLPMD ECKAECALDL SGRPWIKFNA CFKRDKVGDF
     STELTEHFFQ SLAFSMLATL HLNVTGNNDH HKIESLFKAF GRTLRQAIRI EGNEMPSSKG
     VL
//
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