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Protein

Cytochrome c3

Gene
N/A
Organism
Desulfovibrio gigas
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.

Cofactori

heme1 PublicationNote: Binds 4 heme groups covalently per monomer.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi26 – 261Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi29 – 291Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Binding sitei34 – 341Heme 1 (covalent)Combined sources
Binding sitei37 – 371Heme 1 (covalent)Combined sources
Metal bindingi38 – 381Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi39 – 391Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Binding sitei49 – 491Heme 2 (covalent); atypicalCombined sources
Binding sitei54 – 541Heme 2 (covalent); atypicalCombined sources
Metal bindingi55 – 551Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Metal bindingi73 – 731Iron (heme 4 axial ligand); via tele nitrogenCombined sources
Binding sitei83 – 831Heme 3 (covalent)Combined sources
Binding sitei86 – 861Heme 3 (covalent)Combined sources
Metal bindingi87 – 871Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Binding sitei104 – 1041Heme 4 (covalent); atypicalCombined sources
Binding sitei109 – 1091Heme 4 (covalent); atypicalCombined sources
Metal bindingi110 – 1101Iron (heme 4 axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Sulfate respiration, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c3
OrganismiDesulfovibrio gigas
Taxonomic identifieri879 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 112112Cytochrome c3PRO_0000108360Add
BLAST

Structurei

Secondary structure

1
112
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi22 – 243Combined sources
Helixi27 – 293Combined sources
Helixi34 – 363Combined sources
Turni43 – 464Combined sources
Beta strandi49 – 557Combined sources
Beta strandi60 – 623Combined sources
Helixi68 – 736Combined sources
Helixi83 – 919Combined sources
Helixi95 – 1028Combined sources
Beta strandi104 – 1096Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QN0NMR-A1-112[»]
1QN1NMR-A1-112[»]
1WADX-ray1.80A1-112[»]
ProteinModelPortaliP00133.
SMRiP00133. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00133.

Family & Domainsi

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 1 hit.
[Graphical view]
PRINTSiPR00609. CYTOCHROMEC3.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VDVPADGAKI DFIAGGEKNL TVVFNHSTHK DVKCDDCHHD PGDKQYAGCT
60 70 80 90 100
TDGCHNILDK ADKSVNSWYK VVHDAKGGAK PTCISCHKDK AGDDKELKKK
110
LTGCKGSACH PS
Length:112
Mass (Da):11,978
Last modified:July 15, 1999 - v2
Checksum:i61FF10231F4C0080
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211Missing AA sequence (PubMed:11947254).Curated

Sequence databases

PIRiA00126. CCDV3G.

Cross-referencesi

Sequence databases

PIRiA00126. CCDV3G.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QN0NMR-A1-112[»]
1QN1NMR-A1-112[»]
1WADX-ray1.80A1-112[»]
ProteinModelPortaliP00133.
SMRiP00133. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00133.

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 1 hit.
[Graphical view]
PRINTSiPR00609. CYTOCHROMEC3.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The structure of cytochrome c'-3 from Desulfovibrio gigas (NCIB 9332)."
    Ambler R.P., Bruschi M., le Gall J.
    FEBS Lett. 5:115-117(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759.
  2. Kissinger C.
    Thesis (1989), University of Seattle, United States
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  3. "Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8-A resolution and evidence for a specific calcium-binding site."
    Matias P.M., Morais J., Coelho R., Carrondo M.A., Wilson K., Dauter Z., Sieker L.
    Protein Sci. 5:1342-1354(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), SEQUENCE REVISION TO 21.

Entry informationi

Entry nameiCYC3_DESGI
AccessioniPrimary (citable) accession number: P00133
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1999
Last modified: January 20, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The second and fourth heme binding sites have unusual CXXXXCH motifs.Combined sources1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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 one 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.