HIS7_ECO57
ID HIS7_ECO57 Reviewed; 355 AA.
AC Q9S5G5; Q8X8T1;
DT 24-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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, ECO:0000269|PubMed:16966333};
DE AltName: Full=Histidinol-phosphate phosphatase {ECO:0000303|PubMed:16966333};
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=Z3184, ECs2823;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H- / 184 / EHEC;
RX PubMed=10222209; DOI=10.1006/mpat.1998.0253;
RA Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.;
RT "Analysis of the genes responsible for the O-antigen synthesis in
RT enterohaemorrhagic Escherichia coli O157.";
RL Microb. Pathog. 26:235-247(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-165 IN COMPLEX WITH CALCIUM;
RP MAGNESIUM AND ZINC, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, REGION, AND MUTAGENESIS OF GLU-17.
RX PubMed=16966333; DOI=10.1074/jbc.m604916200;
RA Rangarajan E.S., Proteau A., Wagner J., Hung M.N., Matte A., Cygler M.;
RT "Structural snapshots of Escherichia coli histidinol phosphate phosphatase
RT along the reaction pathway.";
RL J. Biol. Chem. 281:37930-37941(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC 4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:16966333};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:16966333};
CC Note=Binds 2 Mg(2+) ions. Can also use Co(2+) and Mn(2+)ions.
CC {ECO:0000269|PubMed:16966333};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01022,
CC ECO:0000269|PubMed:16966333};
CC -!- ACTIVITY REGULATION: Inhibited by Ca(2+).
CC {ECO:0000269|PubMed:16966333}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=54 uM for histidinol phosphate (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:16966333};
CC KM=54 uM for histidinol phosphate (in the presence of Co(2+))
CC {ECO:0000269|PubMed:16966333};
CC KM=41 uM for histidinol phosphate (in the presence of Zn(2+))
CC {ECO:0000269|PubMed:16966333};
CC KM=52 uM for histidinol phosphate (in the presence of Mn(2+))
CC {ECO:0000269|PubMed:16966333};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC 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-histidine
CC 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. {ECO:0000255|HAMAP-
CC Rule:MF_01022}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB36246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB008676; BAA77743.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG57081.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36246.1; ALT_INIT; Genomic_DNA.
DR PIR; E85827; E85827.
DR PIR; G90981; G90981.
DR RefSeq; NP_310850.2; NC_002695.1.
DR RefSeq; WP_000080139.1; NZ_SWKA01000005.1.
DR PDB; 2FPR; X-ray; 1.70 A; A/B=2-165.
DR PDB; 2FPS; X-ray; 2.20 A; A/B=2-165.
DR PDB; 2FPU; X-ray; 1.80 A; A/B=2-165.
DR PDB; 2FPW; X-ray; 1.75 A; A/B=2-165.
DR PDB; 2FPX; X-ray; 1.80 A; A/B=2-165.
DR PDBsum; 2FPR; -.
DR PDBsum; 2FPS; -.
DR PDBsum; 2FPU; -.
DR PDBsum; 2FPW; -.
DR PDBsum; 2FPX; -.
DR AlphaFoldDB; Q9S5G5; -.
DR SMR; Q9S5G5; -.
DR STRING; 155864.EDL933_3094; -.
DR EnsemblBacteria; AAG57081; AAG57081; Z3184.
DR EnsemblBacteria; BAB36246; BAB36246; ECs_2823.
DR GeneID; 914091; -.
DR KEGG; ece:Z3184; -.
DR KEGG; ecs:ECs_2823; -.
DR PATRIC; fig|386585.9.peg.2958; -.
DR eggNOG; COG0131; Bacteria.
DR eggNOG; COG0241; Bacteria.
DR HOGENOM; CLU_044308_0_0_6; -.
DR OMA; PEDTFWP; -.
DR SABIO-RK; Q9S5G5; -.
DR UniPathway; UPA00031; UER00011.
DR UniPathway; UPA00031; UER00013.
DR EvolutionaryTrace; Q9S5G5; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07914; IGPD; 1.
DR Gene3D; 3.30.230.40; -; 2.
DR Gene3D; 3.40.50.1000; -; 1.
DR HAMAP; MF_01022; Bifunc_HisB; 1.
DR HAMAP; MF_00076; HisB; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR020566; His_synth_bifunc_HisB.
DR InterPro; IPR005954; HisB_N.
DR InterPro; IPR006543; Histidinol-phos.
DR InterPro; IPR038494; IGPD_sf.
DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR InterPro; IPR013954; PNK3P.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR23133; PTHR23133; 1.
DR Pfam; PF00475; IGPD; 1.
DR Pfam; PF08645; PNK3P; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Lyase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Reference proteome; Zinc.
FT CHAIN 1..355
FT /note="Histidine biosynthesis bifunctional protein HisB"
FT /id="PRO_0000158208"
FT REGION 1..166
FT /note="Histidinol-phosphatase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT REGION 167..355
FT /note="Imidazoleglycerol-phosphate dehydratase"
FT /evidence="ECO:0000250|UniProtKB:P06987, ECO:0000255|HAMAP-
FT Rule:MF_01022"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000305|PubMed:16966333"
FT ACT_SITE 11
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000305|PubMed:16966333"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01022,
FT ECO:0000269|PubMed:16966333"
FT MUTAGEN 17
FT /note="E->A: Severe decrease in histidinol-phosphate
FT phosphatase activity in presence of low magnesium
FT concentration. At higher magnesium concentration (5mM), no
FT effect on activity."
FT /evidence="ECO:0000269|PubMed:16966333"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2FPR"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:2FPR"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2FPU"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2FPR"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2FPR"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 66..82
FT /evidence="ECO:0007829|PDB:2FPR"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2FPR"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2FPR"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:2FPR"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2FPR"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2FPR"
FT HELIX 155..161
FT /evidence="ECO:0007829|PDB:2FPR"
SQ 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
