AC   MF_00372;
DC   Protein; auto
TR   HAMAP; MF_00372; -; 1; level=0
XX
Names: HutI
XX
ID   HUTI
DE   RecName: Full=Imidazolonepropionase;
DE            EC=3.5.2.7;
DE   AltName: Full=Imidazolone-5-propionate hydrolase;
GN   Name=hutI;
XX
CC   -!- FUNCTION: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond
CC       in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is
CC       the third step in the universal histidine degradation pathway.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate;
CC         Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928,
CC         ChEBI:CHEBI:77893; EC=3.5.2.7;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034;
CC       Note=Binds 1 zinc or iron ion per subunit.;
end case
CC   -!- PATHWAY: Amino-acid degradation; L-histidine degradation into L-
CC       glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       HutI family.
XX
DR   Pfam; PF01979; Amidohydro_1; 1; trigger=no
DR   NCBIfam; TIGR01224; HutI; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   Histidine metabolism
case <FTGroup:1>
KW   Metal-binding
KW   Iron
KW   Zinc
end case
XX
GO   GO:0050480; F:imidazolonepropionase activity
GO   GO:0006548; P:histidine catabolic process
case <FTGroup:1>
GO   GO:0005506; F:iron ion binding
GO   GO:0008270; F:zinc ion binding
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: HUTI_BACSU (P42084)
FT   BINDING         80
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT   Group: 1; Condition: H
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         82
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT   Group: 1; Condition: H
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         249
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT   Group: 1; Condition: H
FT   BINDING         249
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         324
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT   Group: 1; Condition: [DN]
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: [DN]
FT   BINDING         89
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT   Condition: R
FT   BINDING         152
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT   Condition: Y
FT   BINDING         152
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT   Condition: Y
FT   BINDING         185
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT   Condition: H
FT   BINDING         252
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT   Condition: [EQ]
FT   BINDING         326
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT   Condition: N
FT   BINDING         328
FT                   /ligand="N-formimidoyl-L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:58928"
FT   Condition: G
FT   BINDING         329
FT                   /ligand="4-imidazolone-5-propanoate"
FT                   /ligand_id="ChEBI:CHEBI:77893"
FT   Condition: [TS]
XX
Size: 388-456;
Related: None;
Template: P42084; Q8U8Z6; A0KF84;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: MF_00229 (hutH)
Duplicate: None
Plasmid: in AGRRH, RHIME
Comments: None
XX
# Revision 1.33 2023/06/01
//