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Protein

Basic cytochrome c3

Gene
N/A
Organism
Desulfovibrio africanus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Exchanges electrons with [NiFe] and [Fe] hydrogenases and with the acidic cytochrome c3. Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341CalciumCombined sources1 Publication
Metal bindingi36 – 361Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi44 – 441CalciumCombined sources1 Publication
Metal bindingi45 – 451Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi51 – 511Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication
Metal bindingi54 – 541Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei64 – 641Heme 1 (covalent)Combined sources1 Publication
Binding sitei67 – 671Heme 1 (covalent)Combined sources1 Publication
Metal bindingi68 – 681Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication
Metal bindingi69 – 691Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei80 – 801Heme 2 (covalent); atypicalCombined sources1 Publication
Binding sitei85 – 851Heme 2 (covalent); atypicalCombined sources1 Publication
Metal bindingi86 – 861Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication
Metal bindingi107 – 1071Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei114 – 1141Heme 3 (covalent)Combined sources1 Publication
Binding sitei117 – 1171Heme 3 (covalent)Combined sources1 Publication
Metal bindingi118 – 1181Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei133 – 1331Heme 4 (covalent)Combined sources1 Publication
Binding sitei136 – 1361Heme 4 (covalent)Combined sources1 Publication
Metal bindingi137 – 1371Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Sulfate respiration, Transport

Keywords - Ligandi

Calcium, Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Basic cytochrome c3
OrganismiDesulfovibrio africanus
Taxonomic identifieri873 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 140117Basic cytochrome c3PRO_0000006503Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi690850.Desaf_1770.

Structurei

Secondary structure

1
140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Helixi41 – 433Combined sources
Beta strandi47 – 493Combined sources
Helixi52 – 576Combined sources
Helixi61 – 655Combined sources
Beta strandi73 – 753Combined sources
Beta strandi80 – 823Combined sources
Helixi102 – 1076Combined sources
Beta strandi108 – 1103Combined sources
Helixi114 – 1218Combined sources
Helixi122 – 1243Combined sources
Helixi133 – 1375Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BQ4X-ray1.68A/B25-140[»]
ProteinModelPortaliP94691.
SMRiP94691. Positions 25-139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94691.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105XNI. Bacteria.
ENOG41121XT. LUCA.

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.

P94691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLFSMLVA AALVGTMAMA AQAVPQVPAD VVIDHLSNPN AKLEYKVKFS
60 70 80 90 100
HKAHASLGTD AAACQKCHHK WDGKSEIGGC ATEGCHADTT SFKATEKDPK
110 120 130 140
FLMTAFHSKS PMSCQGCHKE MKTAKKTTGP TACAQCHNQK
Length:140
Mass (Da):14,975
Last modified:May 1, 1997 - v1
Checksum:iEA2A805423F416D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661K → S AA sequence (PubMed:8573595).Curated

Mass spectrometryi

Molecular mass is 15102 Da from positions 23 - 140. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09717 Genomic DNA. Translation: CAA70883.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09717 Genomic DNA. Translation: CAA70883.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BQ4X-ray1.68A/B25-140[»]
ProteinModelPortaliP94691.
SMRiP94691. Positions 25-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi690850.Desaf_1770.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105XNI. Bacteria.
ENOG41121XT. LUCA.

Miscellaneous databases

EvolutionaryTraceiP94691.

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. "Further characterization of the two tetraheme cytochromes c3 from Desulfovibiro africanus: nucleotide sequences, EPR spectroscopy and biological activity."
    Magro V., Pieulle L., Forget N., Guigliarelli B., Petillot Y., Hatchikian E.C.
    Biochim. Biophys. Acta 1342:149-163(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, MASS SPECTROMETRY.
    Strain: ATCC 19996 / DSM 2603 / NCIB 8401 / Benghazi.
  2. "Biochemical studies of the c-type cytochromes of the sulfate reducer Desulfovibrio africanus. Characterization of two tetraheme cytochromes c3 with different specificity."
    Pieulle L., Haladjian J., Bonicel J., Hatchikian E.C.
    Biochim. Biophys. Acta 1273:51-61(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-78, FUNCTION, HEME-BINDING.
    Strain: ATCC 19996 / DSM 2603 / NCIB 8401 / Benghazi.
  3. "The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway."
    Pieulle L., Morelli X., Gallice P., Lojou E., Barbier P., Czjzek M., Bianco P., Guerlesquin F., Hatchikian E.C.
    J. Mol. Biol. 354:73-90(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 25-140 IN COMPLEX WITH CALCIUM AND HEME.

Entry informationi

Entry nameiCYC3B_DESAF
AccessioniPrimary (citable) accession number: P94691
Secondary accession number(s): Q9R4E8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 1997
Last modified: January 20, 2016
This is version 94 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 heme binding site has an unusual CXXXXCH motif.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.