Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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Haem_bd Haem-binding domain

SMART accession number:	SM01235
Description:	This domain contains a potential haem-binding motif, CXXCH (PMID:17288564).
Interpro abstract (IPR025992):	This domain contains a potential haem-binding motif, CXXCH [ (PUBMED:17288564) ] and it is often found in association with and .
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 2010 Haem_bd domains in 2010 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Haem_bd domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Haem_bd domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Haem_bd domain in the selected taxonomic class.

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Yamada H, Takashima E, Konishi K
  • Molecular characterization of the membrane-bound quinol peroxidase functionallyconnected to the respiratory chain.
  • FEBS J. 2007; 274: 853-66
  • Display abstract

  • Here, we report for the first time quinol peroxidase (QPO), an enzyme that usesubiquinol-1 as an electron donor for the reduction of H(2)O(2) to water. Wepurified QPO to > 90% purity from the membrane fraction of Actinobacillusactinomycetemcomitans. QPO is a 53.6-kDa protein that contains three heme cmolecules. The qpo gene was predicted to encode a putative bacterial cytochrome cperoxidase with N-terminal extensions containing an additional potential hemec-binding motif. Although qpo has high sequence homology to bacterial cytochrome c peroxidases, QPO did not catalyze peroxidation in the presence of horse heartcytochrome c. In addition, the cytoplasmic membrane of A. actinomycetemcomitanshad apparent QPO-dependent peroxidase activity in the presence of NADH orsuccinate, which are substrates for the respiratory chain. Based on thesefindings, we present a new mechanism for the scavenging of reactive oxygenspecies in which quinol in the respiratory chain is consumed.

• Links (links to other resources describing this domain)

• PFAM	Haem_bd
  INTERPRO	IPR025992

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