HAMAP rule MF_00372
General rule information
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| Accession | MF_00372 |
| Dates | 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 33) |
| Name | HutI |
| Scope(s) |
Bacteria Archaea |
| Template(s) | P42084 (HUTI_BACSU); Q8U8Z6 (HUTI_AGRFC); A0KF84 (HUTI_AERHH); [ Recover all ] |
| Triggered by |
HAMAP; MF_00372 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | HUTI |
| Protein name | RecName: Full=Imidazolonepropionase; EC=3.5.2.7; AltName: Full=Imidazolone-5-propionate hydrolase; |
| Gene name | Name=hutI; |
Comments
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| FUNCTION | Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway. |
| CATALYTIC ACTIVITY | Reaction=4-imidazolone-5-propanoate + H2O = N-formimidoyl-L-glutamate; Xref=Rhea:RHEA:23660, ChEBI:CHEBI:15377, ChEBI:CHEBI:58928, ChEBI:CHEBI:77893; EC=3.5.2.7; |
| case <FTGroup:1> | |
| COFACTOR | Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Note=Binds 1 zinc or iron ion per subunit.; |
| end case | |
| PATHWAY | Amino-acid degradation; L-histidine degradation into L- glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. |
| SUBCELLULAR LOCATION | Cytoplasm. |
| SIMILARITY | Belongs to the metallo-dependent hydrolases superfamily. HutI family. |
Keywords
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| Cytoplasm | |
| Hydrolase | |
| Histidine metabolism | |
| case <FTGroup:1> | |
| Metal-binding | |
| Iron | |
| Zinc | |
| end case | |
Gene Ontology
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| GO:0050480; Molecular function:imidazolonepropionase activity | |
| GO:0006548; Biological process:histidine catabolic process | |
| case <FTGroup:1> | |
| GO:0005506; Molecular function:iron ion binding | |
| GO:0008270; Molecular function:zinc ion binding | |
| end case | |
| GO:0005737; Cellular component:cytoplasm | |
Cross-references
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Features
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| From: HUTI_BACSU (P42084) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 80 | 80 | /ligand="Fe(3+)" /ligand_id="ChEBI:CHEBI:29034" |
H | 1 | |||||||
| BINDING | 80 | 80 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 82 | 82 | /ligand="Fe(3+)" /ligand_id="ChEBI:CHEBI:29034" |
H | 1 | |||||||
| BINDING | 82 | 82 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 249 | 249 | /ligand="Fe(3+)" /ligand_id="ChEBI:CHEBI:29034" |
H | 1 | |||||||
| BINDING | 249 | 249 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
H | 1 | |||||||
| BINDING | 324 | 324 | /ligand="Fe(3+)" /ligand_id="ChEBI:CHEBI:29034" |
[DN] | 1 | |||||||
| BINDING | 324 | 324 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
[DN] | 1 | |||||||
| BINDING | 89 | 89 | /ligand="4-imidazolone-5-propanoate" /ligand_id="ChEBI:CHEBI:77893" |
R | ||||||||
| BINDING | 152 | 152 | /ligand="4-imidazolone-5-propanoate" /ligand_id="ChEBI:CHEBI:77893" |
Y | ||||||||
| BINDING | 152 | 152 | /ligand="N-formimidoyl-L-glutamate" /ligand_id="ChEBI:CHEBI:58928" |
Y | ||||||||
| BINDING | 185 | 185 | /ligand="4-imidazolone-5-propanoate" /ligand_id="ChEBI:CHEBI:77893" |
H | ||||||||
| BINDING | 252 | 252 | /ligand="4-imidazolone-5-propanoate" /ligand_id="ChEBI:CHEBI:77893" |
[EQ] | ||||||||
| BINDING | 326 | 326 | /ligand="N-formimidoyl-L-glutamate" /ligand_id="ChEBI:CHEBI:58928" |
N | ||||||||
| BINDING | 328 | 328 | /ligand="N-formimidoyl-L-glutamate" /ligand_id="ChEBI:CHEBI:58928" |
G | ||||||||
| BINDING | 329 | 329 | /ligand="4-imidazolone-5-propanoate" /ligand_id="ChEBI:CHEBI:77893" |
[TS] | ||||||||
Additional information
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| Size range | 388-456 amino acids |
| Related rules |
None |
| Fusion | Nter: <Unknown> Cter: MF_00229 (hutH) |