Q9KL41 · HUTZ_VIBCH

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).

Catalytic activity

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).

Features

Showing features for site, binding site.

TypeIDPosition(s)Description
Site132Important for activity
Binding site170Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Molecular Functioncoenzyme F420 binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity, acting on the CH-CH group of donors

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Heme oxygenase HutZ
  • EC number
  • Alternative names
    • Heme-degrading enzyme HutZ

Gene names

    • Name
      hutZ
    • Ordered locus names
      VC_A0907

Organism names

Accessions

  • Primary accession
    Q9KL41

Proteomes

Phenotypes & Variants

Disruption phenotype

Mutant is defective in heme utilization.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis272-fold decrease in the amount of liberated Fe2+.
Mutagenesis63Cannot bind heme; when associated with A-170.
Mutagenesis132At pH 8.0, does not affect heme affinity and activity. At pH 6.0, shows a significant reduction in affinity for heme.
Mutagenesis132At pH 8.0, slight decrease in heme affinity. Almost complete loss of heme degradation activity.
Mutagenesis170Can still bind heme. Retains heme degradation activity, but it eliminates pH-dependent activation. Cannot bind heme; when associated with L-63.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004464451-176Heme oxygenase HutZ

Expression

Induction

Negatively regulated by iron.

Interaction

Subunit

Homodimer (PubMed:22627893, PubMed:23013214).
Interacts with HutX, leading to the transfer of the heme from HutX to apo-HutZ (PubMed:26807477).

Protein-protein interaction databases

Chemistry

Family & Domains

Sequence similarities

Belongs to the heme oxygenase HugZ/HutZ family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    176
  • Mass (Da)
    20,300
  • Last updated
    2000-10-01 v1
  • Checksum
    361E569BF68A0A9A
MDQQVKQERLQGRLEPEIKEFRQERKTLQLATVDAQGRPNVSYAPFVQNQEGYFVLISHIARHARNLEVNPQVSIMMIEDETEAKQLFARKRLTFDAVASMVERDSELWCQVIAQMGERFGEIIDGLSQLQDFMLFRLQPEQGLFVKGFGQAYQVSGDDLVDFVHLEEGHRKISNG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE003853
EMBL· GenBank· DDBJ
AAF96804.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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