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-MAY-2013, entry version 45.
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=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 -!- 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.
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DR EMBL; CP000672; ABR00039.1; -; Genomic_DNA.
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; EMVPHFF; -.
DR ProtClustDB; PRK05446; -.
DR BioCyc; HINF374931:GJA4-966-MONOMER; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
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 activity; IEA:HAMAP.
DR GO; GO:0016311; P:dephosphorylation; IEA:GOC.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.1000; -; 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; SSF56784; HAD-like_dom; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 2.
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
//
