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Protein

Cytochrome c3

Gene

DVU_3171

Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron (heme 1 axial ligand)
Metal bindingi47 – 471Iron (heme 3 axial ligand)
Binding sitei52 – 521Heme 1 (covalent)
Binding sitei55 – 551Heme 1 (covalent)
Metal bindingi56 – 561Iron (heme 1 axial ligand)
Metal bindingi57 – 571Iron (heme 2 axial ligand)
Binding sitei68 – 681Heme 2 (covalent); atypical
Binding sitei73 – 731Heme 2 (covalent); atypical
Metal bindingi74 – 741Iron (heme 2 axial ligand)
Metal bindingi92 – 921Iron (heme 4 axial ligand)
Binding sitei101 – 1011Heme 3 (covalent)
Binding sitei104 – 1041Heme 3 (covalent)
Metal bindingi105 – 1051Iron (heme 3 axial ligand)
Binding sitei122 – 1221Heme 4 (covalent); atypical
Binding sitei127 – 1271Heme 4 (covalent); atypical
Metal bindingi128 – 1281Iron (heme 4 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

Enzyme and pathway databases

BioCyciDVUL882:GJIL-3254-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c3
Gene namesi
Ordered Locus Names:DVU_3171
OrganismiDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Taxonomic identifieri882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002194 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 22222 PublicationsAdd
BLAST
Chaini23 – 129107Cytochrome c31 PublicationPRO_0000006504Add
BLAST

Post-translational modificationi

Binds 4 heme groups per subunit.

Proteomic databases

PaxDbiP00131.

Interactioni

Protein-protein interaction databases

STRINGi882.DVU3171.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Beta strandi35 – 384Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 473Combined sources
Beta strandi48 – 503Combined sources
Helixi52 – 543Combined sources
Beta strandi60 – 634Combined sources
Turni70 – 723Combined sources
Beta strandi83 – 853Combined sources
Helixi87 – 926Combined sources
Beta strandi95 – 984Combined sources
Helixi101 – 1099Combined sources
Helixi113 – 1208Combined sources
Beta strandi122 – 1276Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2INMR-A23-129[»]
1GX7NMR-E23-129[»]
1MDVX-ray2.30A/B23-129[»]
2BPNNMR-A23-129[»]
2CTHX-ray1.67A/B23-129[»]
2CYMX-ray2.00A23-129[»]
ProteinModelPortaliP00131.
SMRiP00131. Positions 23-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00131.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106BES. Bacteria.
ENOG410XXW1. LUCA.
OMAiKELTGCK.
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.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00131-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLFFCGVL ALAVAFALPV VAAPKAPADG LKMEATKQPV VFNHSTHKSV
60 70 80 90 100
KCGDCHHPVN GKEDYRKCGT AGCHDSMDKK DKSAKGYYHV MHDKNTKFKS
110 120
CVGCHVEVAG ADAAKKKDLT GCKKSKCHE
Length:129
Mass (Da):13,976
Last modified:August 13, 1987 - v1
Checksum:i78C2A85F33B18441
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04304 Genomic DNA. Translation: CAA27847.1.
AE017285 Genomic DNA. Translation: AAS97641.1.
PIRiA24799. CCDV3.
RefSeqiWP_010940429.1. NC_002937.3.
YP_012381.1. NC_002937.3.

Genome annotation databases

EnsemblBacteriaiAAS97641; AAS97641; DVU_3171.
GeneIDi2795876.
KEGGidvu:DVU3171.
PATRICi32065884. VBIDesVul119526_2876.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04304 Genomic DNA. Translation: CAA27847.1.
AE017285 Genomic DNA. Translation: AAS97641.1.
PIRiA24799. CCDV3.
RefSeqiWP_010940429.1. NC_002937.3.
YP_012381.1. NC_002937.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2INMR-A23-129[»]
1GX7NMR-E23-129[»]
1MDVX-ray2.30A/B23-129[»]
2BPNNMR-A23-129[»]
2CTHX-ray1.67A/B23-129[»]
2CYMX-ray2.00A23-129[»]
ProteinModelPortaliP00131.
SMRiP00131. Positions 23-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi882.DVU3171.

Proteomic databases

PaxDbiP00131.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS97641; AAS97641; DVU_3171.
GeneIDi2795876.
KEGGidvu:DVU3171.
PATRICi32065884. VBIDesVul119526_2876.

Phylogenomic databases

eggNOGiENOG4106BES. Bacteria.
ENOG410XXW1. LUCA.
OMAiKELTGCK.
OrthoDBiEOG6Q2SNC.

Enzyme and pathway databases

BioCyciDVUL882:GJIL-3254-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00131.

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

« Hide 'large scale' publications
  1. "Cloning and sequencing of the gene encoding cytochrome c3 from Desulfovibrio vulgaris (Hildenborough)."
    Voordouw G., Brenner S.
    Eur. J. Biochem. 159:347-351(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Hildenborough / ATCC 29579 / NCIMB 8303.
  3. "Amino acid sequence of cytochrome c3 from Desulfovibrio vulgaris."
    Trousil E.B., Campbell L.L.
    J. Biol. Chem. 249:386-393(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-129.
  4. "Rapid comparison of the cytochrome c3 gene from nine strains of Desulfovibrio vulgaris using polymerase chain reaction amplification."
    Kwoh D.Y., Vedvick T.S., McCue A.F., Gevertz D.
    Can. J. Microbiol. 39:402-411(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-44.
  5. "Effects of amino acid substitution on three-dimensional structure: an X-ray analysis of cytochrome c3 from Desulfovibrio vulgaris Hildenborough at 2-A resolution."
    Morimoto Y., Tani T., Okumura H., Higuchi Y., Yasuoka N.
    J. Biochem. 110:532-540(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  6. "Structure analysis of cytochrome c3 from Desulfovibrio vulgaris Hildenborough at 1.9-A resolution."
    Matias P.M., Frazao C., Morais J., Coll M., Carrondo M.A.
    J. Mol. Biol. 234:680-699(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  7. Simoes P., Matias P.M., Morais J., Wilson K., Dauter Z., Carrondo M.A.
    Submitted (JUN-1997) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS).
  8. "Key role of phenylalanine 20 in cytochrome c3: structure, stability, and function studies."
    Dolla A., Arnoux P., Protasevich I., Lobachov V., Brugna M., Giudici-Orticoni M.-T., Haser R., Czjzek M., Makarov A., Bruschi M.
    Biochemistry 38:33-41(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  9. "Assignment of the redox potentials to the four haems in Desulfovibrio vulgaris cytochrome c3 by 2D-NMR."
    Salgueiro C.A., Turner D.L., Santos H., Legall J., Xavier A.V.
    FEBS Lett. 314:155-158(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity."
    Messias A.C., Kastrau D.H.W., Costa H.S., Legall J., Turner D.L., Santos H., Xavier A.V.
    J. Mol. Biol. 281:719-739(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiCYC3_DESVH
AccessioniPrimary (citable) accession number: P00131
Secondary accession number(s): P81150
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: January 20, 2016
This is version 125 of the entry and version 1 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.