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Protein
Submitted name:

Cytochrome c3

Gene

cytc3

Organism
Desulfovibrio desulfuricans
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi43 – 431Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi46 – 461Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Binding sitei51 – 511Heme 1 (covalent)Combined sources
Binding sitei54 – 541Heme 1 (covalent)Combined sources
Metal bindingi55 – 551Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi56 – 561Iron (heme 4 axial ligand); via tele nitrogenCombined sources
Binding sitei67 – 671Heme 4 (covalent)Combined sources
Binding sitei72 – 721Heme 4 (covalent)Combined sources
Metal bindingi73 – 731Iron (heme 4 axial ligand); via tele nitrogenCombined sources
Metal bindingi90 – 901Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Binding sitei100 – 1001Heme 3 (covalent)Combined sources
Binding sitei103 – 1031Heme 3 (covalent)Combined sources
Metal bindingi104 – 1041Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Binding sitei121 – 1211Heme 2 (covalent)Combined sources
Binding sitei126 – 1261Heme 2 (covalent)Combined sources
Metal bindingi127 – 1271Iron (heme 2 axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Submitted name:
Cytochrome c3Imported
Gene namesi
Name:cytc3Imported
OrganismiDesulfovibrio desulfuricansImported
Taxonomic identifieri876 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 128107Sequence analysisPRO_5004328739Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi525146.Ddes_2013.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GM4X-ray2.05A22-128[»]
1GMBX-ray2.00A22-128[»]
1I77X-ray1.95A22-128[»]
1UP9X-ray1.35A22-128[»]
1UPDX-ray1.40A22-128[»]
3CYRX-ray1.60A22-128[»]
ProteinModelPortaliQ9L915.
SMRiQ9L915. Positions 22-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9L915.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 124100Cytochrom_CIIIInterPro annotationAdd
BLAST

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

eggNOGiENOG4106BES. Bacteria.
ENOG410XXW1. LUCA.
OrthoDBiEOG6Q2SNC.

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.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9L915-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKTLALTCM LALLLAVSAW AAPAVPDKPV EVKGSQKTVM FPHAPHEKVE
60 70 80 90 100
CVTCHHLVDG KESYAKCGSS GCHDDLTAKK GEKSLYYVVH AKGELKHTSC
110 120
LACHSKVVAE KPELKKDLTG CAKSKCHP
Length:128
Mass (Da):13,795
Last modified:March 1, 2001 - v2
Checksum:i5091922B06293FD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187324 Genomic DNA. Translation: AAF43894.2.

Genome annotation databases

PATRICi21738040. VBIDesDes50650_2352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF187324 Genomic DNA. Translation: AAF43894.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GM4X-ray2.05A22-128[»]
1GMBX-ray2.00A22-128[»]
1I77X-ray1.95A22-128[»]
1UP9X-ray1.35A22-128[»]
1UPDX-ray1.40A22-128[»]
3CYRX-ray1.60A22-128[»]
ProteinModelPortaliQ9L915.
SMRiQ9L915. Positions 22-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi525146.Ddes_2013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi21738040. VBIDesDes50650_2352.

Phylogenomic databases

eggNOGiENOG4106BES. Bacteria.
ENOG410XXW1. LUCA.
OrthoDBiEOG6Q2SNC.

Miscellaneous databases

EvolutionaryTraceiQ9L915.

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.
ProtoNetiSearch...

Publicationsi

  1. "Refinement of the Three-Dimensional Structures of Cytochrome C3 from Desulfovibrio Vulgaris Hildenborough at 1.67 Angstroms Resolution and from Desulfovibrio Desulfuricans Atcc 27774 at 1.6 Angstroms Resolution."
    Simoes P., Matias P.M., Morais J., Wilson K., Dauter Z., Carrondo M.A.
    Inorganica Chim Acta 273:213-224(1998)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-128 IN COMPLEX WITH HEME.
  2. "Desulfovibrio desulfuricans ATCC 27774 cytochrome c3 gene."
    da Costa P.N., van Dongen W.M.A.M., Saraiva L.M.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ATCC 27774Imported.
  3. "Spectroscopic investigation and determination of reactivity and structure of the tetraheme cytochrome c3 from Desulfovibrio desulfuricans Essex 6."
    Einsle O., Foerster S., Mann K., Fritz G., Messerschmidt A., Kroneck P.M.
    Eur. J. Biochem. 268:3028-3035(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-128 IN COMPLEX WITH HEME.
  4. "Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome."
    Louro R.O., Bento I., Matias P.M., Catarino T., Baptista A.M., Soares C.M., Carrondo M.A., Turner D.L., Xavier A.V.
    J. Biol. Chem. 276:44044-44051(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 22-128 IN COMPLEX WITH HEME.
  5. "Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized and reduced high-resolution structures at pH 7.6."
    Bento I., Matias P.M., Baptista A.M., da Costa P.N., van Dongen W.M., Saraiva L.M., Schneider T.R., Soares C.M., Carrondo M.A.
    Proteins 54:135-152(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 22-128 IN COMPLEX WITH HEME.

Entry informationi

Entry nameiQ9L915_DESDE
AccessioniPrimary (citable) accession number: Q9L915
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: March 1, 2001
Last modified: March 16, 2016
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.