AC   MF_01022;
DC   Protein; auto
TR   HAMAP; MF_01022; -; 1; level=0
XX
Names: Bifunc_HisB
XX
ID   HIS7
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;
XX
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
end case
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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.
XX
DR   Pfam; PF00475; IGPD; 1; trigger=no
DR   Pfam; PF08645; PNK3P; 1; trigger=no
DR   NCBIfam; TIGR01662; HAD-SF-IIIA; 1; trigger=no
DR   NCBIfam; TIGR01261; HisB_Nterm; 1; trigger=no
DR   NCBIfam; TIGR01656; Histidinol-ppas; 1; trigger=no
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1; trigger=no
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Cytoplasm
KW   Histidine biosynthesis
KW   Hydrolase
KW   Lyase
KW   Magnesium
KW   Metal-binding
KW   Multifunctional enzyme
case <FTGroup:1>
KW   Zinc
end case
XX
GO   GO:0004401; F:histidinol-phosphatase activity
GO   GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity
GO   GO:0000105; P:histidine biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: HIS7_ECO57 (Q9S5G5)
FT   REGION          Nter..166
FT                   /note="Histidinol-phosphatase"
FT   REGION          167..Cter
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT   Condition: D
FT   ACT_SITE        11
FT                   /note="Proton donor"
FT   Condition: D
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: H
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Optional; Group: 1; Condition: C
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
XX
Size: 350-390;
Related: MF_00076;
Template: Q9S5G5; P06987;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.32 2023/06/01
//