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Protein

Cytochrome c3

Gene

cyd

Organism
Desulfuromonas acetoxidans (Chloropseudomonas ethylica)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

Redox potential

E0 are -140 mV, -210 mV and -240 mV.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi17 – 171Iron (heme 1 axial ligand)
Metal bindingi20 – 201Iron (heme 2 axial ligand)
Binding sitei26 – 261Heme 1 (covalent)
Binding sitei29 – 291Heme 1 (covalent)
Metal bindingi30 – 301Iron (heme 1 axial ligand)
Metal bindingi45 – 451Iron (heme 3 axial ligand)
Binding sitei49 – 491Heme 2 (covalent)
Binding sitei52 – 521Heme 2 (covalent)
Metal bindingi53 – 531Iron (heme 2 axial ligand)
Binding sitei62 – 621Heme 3 (covalent)
Binding sitei65 – 651Heme 3 (covalent)
Metal bindingi66 – 661Iron (heme 3 axial ligand)

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
Alternative name(s):
Cytochrome c551.5
Cytochrome c7
Gene namesi
Name:cyd
OrganismiDesulfuromonas acetoxidans (Chloropseudomonas ethylica)
Taxonomic identifieri891 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesDesulfuromonadaceaeDesulfuromonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6868Cytochrome c3PRO_0000108364Add
BLAST

Post-translational modificationi

Binds 3 heme groups per subunit.

Structurei

Secondary structure

1
68
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi9 – 113Combined sources
Beta strandi13 – 164Combined sources
Helixi17 – 248Combined sources
Helixi26 – 283Combined sources
Beta strandi30 – 334Combined sources
Helixi41 – 444Combined sources
Turni45 – 495Combined sources
Helixi50 – 534Combined sources
Beta strandi56 – 583Combined sources
Helixi62 – 654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EHJNMR-A1-68[»]
1F22NMR-A1-68[»]
1HH5X-ray1.90A1-68[»]
1KWJNMR-A1-68[»]
1L3ONMR-A1-68[»]
1LM2NMR-A1-68[»]
1NEWNMR-A1-68[»]
ProteinModelPortaliP00137.
SMRiP00137. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00137.

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.

Sequencei

Sequence statusi: Complete.

P00137-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADVVTYENKK GNVTFDHKAH AEKLGCDACH EGTPAKIAID KKSAHKDACK
60
TCHKSNNGPT KCGGCHIK
Length:68
Mass (Da):7,262
Last modified:July 21, 1986 - v1
Checksum:i6A54074BF1A5DAB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005234 Genomic DNA. Translation: AAC46253.1.
PIRiA00130. CCDS7.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005234 Genomic DNA. Translation: AAC46253.1.
PIRiA00130. CCDS7.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EHJNMR-A1-68[»]
1F22NMR-A1-68[»]
1HH5X-ray1.90A1-68[»]
1KWJNMR-A1-68[»]
1L3ONMR-A1-68[»]
1LM2NMR-A1-68[»]
1NEWNMR-A1-68[»]
ProteinModelPortaliP00137.
SMRiP00137. Positions 1-68.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00137.

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. "The amino acid sequence of cytochrome c551.5 (cytochrome c-7) from the green photosynthetic bacterium Chloropseudomonas ethylica."
    Ambler R.P.
    FEBS Lett. 18:351-353(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "The Desulfuromonas acetoxidans triheme cytochrome c7 produced in Desulfovibrio desulfuricans retains its metal reductase activity."
    Aubert C., Lojou E., Bianco P., Rousset M., Durand M.C., Bruschi M., Dolla A.
    Appl. Environ. Microbiol. 64:1308-1312(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Assignment of the ligand geometry and redox potentials of the trihaem ferricytochrome c3 from Desulfuromonas acetoxidans."
    Turner D.L., Costa H.S., Coutinho I.B., Legall J., Xavier A.V.
    Eur. J. Biochem. 243:474-481(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7."
    Assfalg M., Bertini I., Bruschi M., Michel C., Turano P.
    Proc. Natl. Acad. Sci. U.S.A. 99:9750-9754(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, FUNCTION AS A METAL REDUCTASE.
  5. "Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution."
    Czjzek M., Arnoux P., Haser R., Shepard W.
    Acta Crystallogr. D 57:670-678(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  6. "NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans."
    Banci L., Bertini I., Bruschi M., Sompornpisut P., Turano P.
    Proc. Natl. Acad. Sci. U.S.A. 93:14396-14400(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  7. "800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans."
    Assfalg M., Banci L., Bertini I., Bruschi M., Turano P.
    Eur. J. Biochem. 256:261-270(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  8. "A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans: comparison between the reduced and the oxidized forms."
    Assfalg M., Banci L., Bertini I., Bruschi M., Giudici-Orticoni M.-T., Turano P.
    Eur. J. Biochem. 266:634-643(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  9. "A quick solution structure determination of the fully oxidized double mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic implications."
    Assfalg M., Bertini I., Turano P., Bruschi M., Durand M.C., Giudici-Orticoni M.-T., Dolla A.
    J. Biomol. NMR 22:107-122(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCYC3_DESAC
AccessioniPrimary (citable) accession number: P00137
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 20, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.