Q9KL41 · HUTZ_VIBCH
- ProteinHeme oxygenase HutZ
- GenehutZ
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids176 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in heme degradation (PubMed:15205415, PubMed:22627893, PubMed:28481076, PubMed:28607990).
Catalyzes the degradation of heme to biliverdin, with the release of iron (PubMed:22627893, PubMed:28607990).
Forms biliverdin beta and delta (PubMed:28607990).
Binds heme with high efficiency (PubMed:15205415, PubMed:22627893).
Catalyzes the degradation of heme to biliverdin, with the release of iron (PubMed:22627893, PubMed:28607990).
Forms biliverdin beta and delta (PubMed:28607990).
Binds heme with high efficiency (PubMed:15205415, PubMed:22627893).
Catalytic activity
- 3 AH2 + 2 H+ + heme b + 3 O2 = 3 A + biliverdin IXbeta + CO + Fe2+ + 3 H2O
3 CHEBI:17499 + 2 CHEBI:15378 + CHEBI:60344 + 3 CHEBI:15379 = 3 CHEBI:13193 + CHEBI:136509 + CHEBI:17245 + CHEBI:29033 + 3 CHEBI:15377
Activity regulation
Activity is pH-dependent. A proximal hydrogen bond between Asp-132 and the heme axial ligant His-170 is essential for heme degradation activity (PubMed:28481076).
Heme-degradation reaction is inhibited by iron chelators (PubMed:28352909).
Heme-degradation reaction is inhibited by iron chelators (PubMed:28352909).
Features
Showing features for site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | coenzyme F420 binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the CH-CH group of donors |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHeme oxygenase HutZ
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Vibrionales > Vibrionaceae > Vibrio
Accessions
- Primary accessionQ9KL41
Proteomes
Phenotypes & Variants
Disruption phenotype
Mutant is defective in heme utilization.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 27 | 2-fold decrease in the amount of liberated Fe2+. | ||||
Sequence: T → V | ||||||
Mutagenesis | 63 | Cannot bind heme; when associated with A-170. | ||||
Sequence: H → L | ||||||
Mutagenesis | 132 | At pH 8.0, does not affect heme affinity and activity. At pH 6.0, shows a significant reduction in affinity for heme. | ||||
Sequence: D → E | ||||||
Mutagenesis | 132 | At pH 8.0, slight decrease in heme affinity. Almost complete loss of heme degradation activity. | ||||
Sequence: D → L or N | ||||||
Mutagenesis | 170 | Can still bind heme. Retains heme degradation activity, but it eliminates pH-dependent activation. Cannot bind heme; when associated with L-63. | ||||
Sequence: H → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446445 | 1-176 | Heme oxygenase HutZ | |||
Sequence: MDQQVKQERLQGRLEPEIKEFRQERKTLQLATVDAQGRPNVSYAPFVQNQEGYFVLISHIARHARNLEVNPQVSIMMIEDETEAKQLFARKRLTFDAVASMVERDSELWCQVIAQMGERFGEIIDGLSQLQDFMLFRLQPEQGLFVKGFGQAYQVSGDDLVDFVHLEEGHRKISNG |
Expression
Induction
Negatively regulated by iron.
Structure
Sequence
- Sequence statusComplete
- Length176
- Mass (Da)20,300
- Last updated2000-10-01 v1
- Checksum361E569BF68A0A9A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE003853 EMBL· GenBank· DDBJ | AAF96804.1 EMBL· GenBank· DDBJ | Genomic DNA |