Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) ...
9-478
1.91e-134
Di-haem cytochrome c peroxidase; This is a family of distinct cytochrome c peroxidases (CCPs) that contain two haem groups. Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidisable substrate. However, since they possess two, instead of one, haem prosthetic groups, bacterial CCPs reduce hydrogen peroxide without the need to generate semi-stable free radicals. The two haem groups have significantly different redox potentials. The high potential (+320 mV) haem feeds electrons from electron shuttle proteins to the low potential (-330 mV) haem, where peroxide is reduced (indeed, the low potential site is known as the peroxidatic site). The CCP protein itself is structured into two domains, each containing one c-type haem group, with a calcium-binding site at the domain interface. This family also includes MauG proteins, whose similarity to di-haem CCP was previously recognized.
The actual alignment was detected with superfamily member COG3488:
Pssm-ID: 478002 Cd Length: 461 Bit Score: 396.10 E-value: 1.91e-134
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It ...
41-478
2.24e-91
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It carries the two characteriztic Cys-X-Y-Cys-His haem-binding motifs. The C-terminal high-potential site functions as an electron transfer centre, and the N-terminal low-potential site corresponds to the peroxidatic centre. Its probable function is as a peroxidase.
Pssm-ID: 428995 [Multi-domain] Cd Length: 486 Bit Score: 286.42 E-value: 2.24e-91
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It ...
41-478
2.24e-91
Di-haem oxidoreductase, putative peroxidase; DHOR is a family of di-haem oxidoredictases. It carries the two characteriztic Cys-X-Y-Cys-His haem-binding motifs. The C-terminal high-potential site functions as an electron transfer centre, and the N-terminal low-potential site corresponds to the peroxidatic centre. Its probable function is as a peroxidase.
Pssm-ID: 428995 [Multi-domain] Cd Length: 486 Bit Score: 286.42 E-value: 2.24e-91
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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