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Histidine biosynthesis bifunctional protein HisB [Includes: Histidinol-phosphatase (EC 3.1.3.15) (Histidinol-phosphate phosphatase); Imidazoleglycerol-phosphate dehydratase (IGPD) (EC 4.2.1.19)]

 HIS7_ECO57              Reviewed;         355 AA.
Q9S5G5; Q8X8T1;
24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 120.
RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000255|HAMAP-Rule:MF_01022};
Includes:
RecName: Full=Histidinol-phosphatase {ECO:0000255|HAMAP-Rule:MF_01022};
EC=3.1.3.15 {ECO:0000255|HAMAP-Rule:MF_01022, ECO:0000269|PubMed:16966333};
AltName: Full=Histidinol-phosphate phosphatase {ECO:0000303|PubMed:16966333};
Includes:
RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01022};
Short=IGPD {ECO:0000255|HAMAP-Rule:MF_01022};
EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_01022};
Name=hisB {ECO:0000255|HAMAP-Rule:MF_01022};
OrderedLocusNames=Z3184, ECs2823;
Escherichia coli O157:H7.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83334;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=O157:H- / 184 / EHEC;
PubMed=10222209; DOI=10.1006/mpat.1998.0253;
Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
"Analysis of the genes responsible for the O-antigen synthesis in
enterohaemorrhagic Escherichia coli O157.";
Microb. Pathog. 26:235-247(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
PubMed=11206551; DOI=10.1038/35054089;
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
Welch R.A., Blattner F.R.;
"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
Nature 409:529-533(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
PubMed=11258796; DOI=10.1093/dnares/8.1.11;
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
Kuhara S., Shiba T., Hattori M., Shinagawa H.;
"Complete genome sequence of enterohemorrhagic Escherichia coli
O157:H7 and genomic comparison with a laboratory strain K-12.";
DNA Res. 8:11-22(2001).
[4]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-165 IN COMPLEX WITH
CALCIUM; MAGNESIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, REGION, AND
MUTAGENESIS OF GLU-17.
PubMed=16966333; DOI=10.1074/jbc.M604916200;
Rangarajan E.S., Proteau A., Wagner J., Hung M.N., Matte A.,
Cygler M.;
"Structural snapshots of Escherichia coli histidinol phosphate
phosphatase along the reaction pathway.";
J. Biol. Chem. 281:37930-37941(2006).
-!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3-
phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01022}.
-!- CATALYTIC ACTIVITY: L-histidinol phosphate + H(2)O = L-histidinol
+ phosphate. {ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333};
Note=Binds 2 Mg(2+) ions. Also can use Co(2+) and Mn(2+)ions.
{ECO:0000269|PubMed:16966333};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333};
-!- ENZYME REGULATION: Inhibited by Ca(2+).
{ECO:0000269|PubMed:16966333}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=54 uM for histidinol phosphate (in the presence of Mg(2+))
{ECO:0000269|PubMed:16966333};
KM=54 uM for histidinol phosphate (in the presence of Co(2+))
{ECO:0000269|PubMed:16966333};
KM=41 uM for histidinol phosphate (in the presence of Zn(2+))
{ECO:0000269|PubMed:16966333};
KM=52 uM for histidinol phosphate (in the presence of Mn(2+))
{ECO:0000269|PubMed:16966333};
-!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
{ECO:0000255|HAMAP-Rule:MF_01022}.
-!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
{ECO:0000255|HAMAP-Rule:MF_01022}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01022}.
-!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
phosphatase family. {ECO:0000255|HAMAP-Rule:MF_01022}.
-!- SIMILARITY: In the C-terminal section; belongs to the
imidazoleglycerol-phosphate dehydratase family.
{ECO:0000255|HAMAP-Rule:MF_01022}.
-!- SEQUENCE CAUTION:
Sequence=AAG57081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAB36246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB008676; BAA77743.1; -; Genomic_DNA.
EMBL; AE005174; AAG57081.1; ALT_INIT; Genomic_DNA.
EMBL; BA000007; BAB36246.1; ALT_INIT; Genomic_DNA.
PIR; E85827; E85827.
PIR; G90981; G90981.
RefSeq; NP_310850.2; NC_002695.1.
RefSeq; WP_000080139.1; NZ_NOKN01000002.1.
PDB; 2FPR; X-ray; 1.70 A; A/B=2-165.
PDB; 2FPS; X-ray; 2.20 A; A/B=2-165.
PDB; 2FPU; X-ray; 1.80 A; A/B=2-165.
PDB; 2FPW; X-ray; 1.75 A; A/B=2-165.
PDB; 2FPX; X-ray; 1.80 A; A/B=2-165.
PDBsum; 2FPR; -.
PDBsum; 2FPS; -.
PDBsum; 2FPU; -.
PDBsum; 2FPW; -.
PDBsum; 2FPX; -.
ProteinModelPortal; Q9S5G5; -.
SMR; Q9S5G5; -.
STRING; 155864.Z3184; -.
EnsemblBacteria; AAG57081; AAG57081; Z3184.
EnsemblBacteria; BAB36246; BAB36246; BAB36246.
GeneID; 914091; -.
KEGG; ece:Z3184; -.
KEGG; ecs:ECs2823; -.
PATRIC; fig|386585.9.peg.2958; -.
eggNOG; ENOG4105ECC; Bacteria.
eggNOG; COG0131; LUCA.
eggNOG; COG0241; LUCA.
HOGENOM; HOG000228065; -.
KO; K01089; -.
OMA; PEDTFWP; -.
UniPathway; UPA00031; UER00011.
UniPathway; UPA00031; UER00013.
EvolutionaryTrace; Q9S5G5; -.
Proteomes; UP000000558; Chromosome.
Proteomes; UP000002519; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd07914; IGPD; 1.
Gene3D; 3.30.230.40; -; 2.
Gene3D; 3.40.50.1000; -; 1.
HAMAP; MF_01022; Bifunc_HisB; 1.
HAMAP; MF_00076; HisB; 1.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006549; HAD-SF_hydro_IIIA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR020566; His_synth_bifunc_HisB.
InterPro; IPR005954; HisB_N.
InterPro; IPR006543; Histidinol-phos.
InterPro; IPR038494; IGPD_sf.
InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
InterPro; IPR013954; PNK3P.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
PANTHER; PTHR23133; PTHR23133; 1.
Pfam; PF00475; IGPD; 1.
Pfam; PF08645; PNK3P; 1.
SUPFAM; SSF54211; SSF54211; 2.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1.
TIGRFAMs; TIGR01261; hisB_Nterm; 1.
TIGRFAMs; TIGR01656; Histidinol-ppas; 1.
PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm;
Histidine biosynthesis; Hydrolase; Lyase; Magnesium; Metal-binding;
Multifunctional enzyme; Reference proteome; Zinc.
CHAIN 1 355 Histidine biosynthesis bifunctional
protein HisB.
/FTId=PRO_0000158208.
REGION 1 166 Histidinol-phosphatase.
{ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
REGION 167 355 Imidazoleglycerol-phosphate dehydratase.
{ECO:0000250|UniProtKB:P06987,
ECO:0000255|HAMAP-Rule:MF_01022}.
ACT_SITE 9 9 Nucleophile. {ECO:0000255|HAMAP-
Rule:MF_01022,
ECO:0000305|PubMed:16966333}.
ACT_SITE 11 11 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_01022,
ECO:0000305|PubMed:16966333}.
METAL 9 9 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 11 11 Magnesium; via carbonyl oxygen.
{ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 93 93 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 95 95 Zinc; via pros nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 101 101 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 103 103 Zinc. {ECO:0000255|HAMAP-Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
METAL 130 130 Magnesium. {ECO:0000255|HAMAP-
Rule:MF_01022,
ECO:0000269|PubMed:16966333}.
MUTAGEN 17 17 E->A: Severe decrease in histidinol-
phosphate phosphatase activity in
presence of low magnesium concentration.
At higher magnesium concentration (5mM),
no effect on activity.
{ECO:0000269|PubMed:16966333}.
STRAND 4 8 {ECO:0000244|PDB:2FPR}.
TURN 12 14 {ECO:0000244|PDB:2FPR}.
TURN 19 21 {ECO:0000244|PDB:2FPU}.
HELIX 27 29 {ECO:0000244|PDB:2FPR}.
HELIX 36 45 {ECO:0000244|PDB:2FPR}.
STRAND 48 55 {ECO:0000244|PDB:2FPR}.
TURN 57 60 {ECO:0000244|PDB:2FPR}.
HELIX 66 82 {ECO:0000244|PDB:2FPR}.
STRAND 87 93 {ECO:0000244|PDB:2FPR}.
HELIX 97 99 {ECO:0000244|PDB:2FPR}.
STRAND 102 104 {ECO:0000244|PDB:2FPR}.
HELIX 109 114 {ECO:0000244|PDB:2FPR}.
HELIX 122 124 {ECO:0000244|PDB:2FPR}.
STRAND 126 131 {ECO:0000244|PDB:2FPR}.
HELIX 132 141 {ECO:0000244|PDB:2FPR}.
STRAND 143 147 {ECO:0000244|PDB:2FPR}.
TURN 150 152 {ECO:0000244|PDB:2FPR}.
HELIX 155 161 {ECO:0000244|PDB:2FPR}.
SEQUENCE 355 AA; 40290 MW; 91229A10D62A4EE8 CRC64;
MSQKYLFIDR DGTLISEPPS DFQVDRFDKL AFEPGVIPQL LKLQKAGYKL VMITNQDGLG
TQSFPQADFD GPHNLMMQIF TSQGVQFDEV LICPHLPADE CDCRKPKVKL VERYLAEQAM
DRANSYVIGD RATDIQLAEN MGINGLRYDR ETLNWPMIGE QLTRRDRYAH VVRNTKETQI
DVQVWLDREG GSKINTGVGF FDHMLDQIAT HGGFRMEINV KGDLYIDDHH TVEDTGLALG
EALKIALGDK RGICRFGFVL PMDECLARCA LDISGRPHLE YKAEFTYQRV GDLSTEMIEH
FFRSLSYTMG VTLHLKTKGK NDHHRVESLF KAFGRTLRQA IRVEGDTLPS SKGVL


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