Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Cytochrome c peroxidase

Gene
N/A
Organism
Marinobacter hydrocarbonoclasticus (Pseudomonas nautica)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Cofactori

hemeUniRule annotationNote: Binds 2 heme groups.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511Heme 1 (covalent)UniRule annotationCombined sources
Binding sitei51 – 511Heme 2 (covalent)Combined sources
Binding sitei54 – 541Heme 1 (covalent)UniRule annotation
Binding sitei54 – 541Heme 2 (covalent)Combined sources
Metal bindingi55 – 551Iron (heme 1 axial ligand)UniRule annotation
Metal bindingi55 – 551Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi55 – 551Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Metal bindingi71 – 711Iron (heme 1 axial ligand)UniRule annotation
Metal bindingi71 – 711Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Metal bindingi79 – 791CalciumCombined sources
Sitei94 – 941Important for catalytic activityCombined sources
Active sitei114 – 1141Proton donor/acceptorCombined sources
Binding sitei197 – 1971Heme 2 (covalent)UniRule annotation
Binding sitei197 – 1971Heme 3 (covalent)Combined sources
Binding sitei200 – 2001Heme 2 (covalent)UniRule annotation
Binding sitei200 – 2001Heme 3 (covalent)Combined sources
Metal bindingi201 – 2011Iron (heme 2 axial ligand)UniRule annotation
Metal bindingi201 – 2011Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Metal bindingi256 – 2561Calcium; via carbonyl oxygenCombined sources
Metal bindingi258 – 2581Calcium; via carbonyl oxygenCombined sources
Metal bindingi275 – 2751Iron (heme 2 axial ligand)UniRule annotation
Metal bindingi275 – 2751Iron (heme 3 axial ligand)Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, HemeCombined sources, Iron, Metal-binding

Protein family/group databases

PeroxiBasei5023. MaqDiHCcP_617.

Names & Taxonomyi

Protein namesi
Submitted name:
Cytochrome c peroxidaseImported
OrganismiMarinobacter hydrocarbonoclasticus (Pseudomonas nautica)Imported
Taxonomic identifieri2743 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeMarinobacter

PTM / Processingi

Post-translational modificationi

Binds 2 heme groups per subunit.UniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi351348.Maqu_0372.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NMLX-ray2.20A1-326[»]
1RZ5X-ray2.40A1-326[»]
1RZ6X-ray2.20A1-326[»]
ProteinModelPortaliP83787.
SMRiP83787. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83787.

Family & Domainsi

Family and domain databases

Gene3Di1.10.760.10. 2 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
PF00034. Cytochrom_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 2 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DNLMERANSM FEPIPKYPPV IDGNELTQAK VELGKMEFFE PRLSSSHLIS
60 70 80 90 100
CNTCHNVGLG GDDELPTSIG HGWQKGPRNS PTVFNAVFNA AQFWDGRAAD
110 120 130 140 150
LAEQAKGPVQ AGVEMSSTPD RVVATLKSMP EYIERFEDAF PGQENPVTFD
160 170 180 190 200
NMAVAIEAYE ATLITPEAPF DKYLRGDTSA LNESEKEGLA LFMDRGCTAC
210 220 230 240 250
HSGVNLGGQN YYPFGLVAKP GAEILPEGDK GRFSVTETAS DEYVFRASPL
260 270 280 290 300
RNIELTAPYF HSGAVWSLEE AVAVMGTAQL GTELNNDEVK SIVAFLKTLT
310 320
GNVPEVTYPV LPPSTANTPK PVDMIP
Length:326
Mass (Da):35,355
Last modified:March 15, 2004 - v1
Checksum:iFAAABCAC1E4652FF
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NMLX-ray2.20A1-326[»]
1RZ5X-ray2.40A1-326[»]
1RZ6X-ray2.20A1-326[»]
ProteinModelPortaliP83787.
SMRiP83787. Positions 1-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351348.Maqu_0372.

Protein family/group databases

PeroxiBasei5023. MaqDiHCcP_617.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP83787.

Family and domain databases

Gene3Di1.10.760.10. 2 hits.
InterProiIPR009056. Cyt_c-like_dom.
IPR004852. Di-haem_cyt_c_peroxidsae.
IPR026259. MauG/Cytc_peroxidase.
[Graphical view]
PfamiPF03150. CCP_MauG. 1 hit.
PF00034. Cytochrom_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000294. Cytochrome-c_peroxidase. 1 hit.
SUPFAMiSSF46626. SSF46626. 2 hits.
PROSITEiPS51007. CYTC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617."
    Dias J.M., Alves T., Bonifacio C., Pereira A.S., Trincao J., Bourgeois D., Moura I., Romao M.J.
    Structure 12:961-973(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH CALCIUM AND HEME, ACTIVE SITE.

Entry informationi

Entry nameiP83787_MARHY
AccessioniPrimary (citable) accession number: P83787
Entry historyi
Integrated into UniProtKB/TrEMBL: March 15, 2004
Last sequence update: March 15, 2004
Last modified: June 24, 2015
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.