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Protein
Submitted name:

Cytochrome c

Gene

GSU1996

Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Iron (heme 1 axial ligand); via tele nitrogenCombined sources1
Metal bindingi48Iron (heme 3 axial ligand); via tele nitrogenCombined sources1
Metal bindingi48Iron (heme 7 axial ligand); via tele nitrogenCombined sources1
Binding sitei56Heme 1 (covalent)Combined sources1
Binding sitei59Heme 1 (covalent)Combined sources1
Metal bindingi60Iron (heme 1 axial ligand); via tele nitrogenCombined sources1
Metal bindingi74Iron (heme 2 axial ligand)Combined sources1
Metal bindingi74Iron (heme 4 axial ligand)Combined sources1
Binding sitei83Heme 3 (covalent)Combined sources1
Binding sitei83Heme 7 (covalent)Combined sources1
Binding sitei86Heme 3 (covalent)Combined sources1
Binding sitei86Heme 7 (covalent)Combined sources1
Metal bindingi87Iron (heme 3 axial ligand); via tele nitrogenCombined sources1
Metal bindingi87Iron (heme 7 axial ligand); via tele nitrogenCombined sources1
Binding sitei101Heme 2 (covalent)Combined sources1
Binding sitei101Heme 4 (covalent)Combined sources1
Binding sitei104Heme 2 (covalent)Combined sources1
Binding sitei104Heme 4 (covalent)Combined sources1
Metal bindingi105Iron (heme 2 axial ligand); via tele nitrogenCombined sources1
Metal bindingi105Iron (heme 4 axial ligand); via tele nitrogenCombined sources1
Metal bindingi126Iron (heme 5 axial ligand); via tele nitrogenCombined sources1
Metal bindingi126Iron (heme 6 axial ligand); via tele nitrogenCombined sources1
Metal bindingi129Iron (heme 10 axial ligand); via tele nitrogenCombined sources1
Metal bindingi129Iron (heme 11 axial ligand); via tele nitrogenCombined sources1
Binding sitei137Heme 5 (covalent)Combined sources1
Binding sitei137Heme 6 (covalent)Combined sources1
Binding sitei140Heme 5 (covalent)Combined sources1
Binding sitei140Heme 6 (covalent)Combined sources1
Metal bindingi141Iron (heme 5 axial ligand); via tele nitrogenCombined sources1
Metal bindingi141Iron (heme 6 axial ligand); via tele nitrogenCombined sources1
Metal bindingi154Iron (heme 8 axial ligand)Combined sources1
Metal bindingi154Iron (heme 9 axial ligand)Combined sources1
Binding sitei163Heme 10 (covalent)Combined sources1
Binding sitei163Heme 11 (covalent)Combined sources1
Binding sitei166Heme 10 (covalent)Combined sources1
Binding sitei166Heme 11 (covalent)Combined sources1
Metal bindingi167Iron (heme 10 axial ligand); via tele nitrogenCombined sources1
Metal bindingi167Iron (heme 11 axial ligand); via tele nitrogenCombined sources1
Binding sitei179Heme 8 (covalent)Combined sources1
Binding sitei179Heme 9 (covalent)Combined sources1
Binding sitei182Heme 8 (covalent)Combined sources1
Binding sitei182Heme 9 (covalent)Combined sources1
Metal bindingi183Iron (heme 8 axial ligand); via tele nitrogenCombined sources1
Metal bindingi183Iron (heme 9 axial ligand); via tele nitrogenCombined sources1
Metal bindingi206Iron (heme 12 axial ligand); via tele nitrogenCombined sources1
Metal bindingi209Iron (heme 14 axial ligand); via tele nitrogenCombined sources1
Binding sitei215Heme 12 (covalent)Combined sources1
Binding sitei218Heme 12 (covalent)Combined sources1
Metal bindingi219Iron (heme 12 axial ligand); via tele nitrogenCombined sources1
Metal bindingi234Iron (heme 13 axial ligand)Combined sources1
Binding sitei243Heme 14 (covalent)Combined sources1
Binding sitei246Heme 14 (covalent)Combined sources1
Metal bindingi247Iron (heme 14 axial ligand); via tele nitrogenCombined sources1
Binding sitei259Heme 13 (covalent)Combined sources1
Binding sitei262Heme 13 (covalent)Combined sources1
Metal bindingi263Iron (heme 13 axial ligand); via tele nitrogenCombined sources1
Metal bindingi284Iron (heme 15 axial ligand); via tele nitrogenCombined sources1
Metal bindingi287Iron (heme 17 axial ligand); via tele nitrogenCombined sources1
Metal bindingi287Iron (heme 18 axial ligand); via tele nitrogenCombined sources1
Binding sitei293Heme 15 (covalent)Combined sources1
Binding sitei296Heme 15 (covalent)Combined sources1
Metal bindingi297Iron (heme 15 axial ligand); via tele nitrogenCombined sources1
Metal bindingi312Iron (heme 16 axial ligand)Combined sources1
Binding sitei321Heme 17 (covalent)Combined sources1
Binding sitei321Heme 18 (covalent)Combined sources1
Binding sitei324Heme 17 (covalent)Combined sources1
Binding sitei324Heme 18 (covalent)Combined sources1
Metal bindingi325Iron (heme 17 axial ligand); via tele nitrogenCombined sources1
Metal bindingi325Iron (heme 18 axial ligand); via tele nitrogenCombined sources1
Binding sitei337Heme 16 (covalent)Combined sources1
Binding sitei340Heme 16 (covalent)Combined sources1
Metal bindingi341Iron (heme 16 axial ligand); via tele nitrogenCombined sources1

GO - Molecular functioni

Keywordsi

LigandHemeCombined sources, Iron, Metal-binding

Enzyme and pathway databases

BioCyciGSUL243231:GH27-2199-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Cytochrome cImported
Gene namesi
Ordered Locus Names:GSU1996Imported
OrganismiGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)Imported
Taxonomic identifieri243231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter
Proteomesi
  • UP000000577 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi243231.GSU1996.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RWJX-ray1.70A184-265[»]
3OUEX-ray2.15A186-343[»]
3OUQX-ray2.60A26-186[»]
3OV0X-ray3.20A26-343[»]
ProteinModelPortaliQ74BP5.
SMRiQ74BP5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ74BP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 330Cytochrome cInterPro annotationAdd BLAST280

Phylogenomic databases

eggNOGiENOG4105SNX. Bacteria.
ENOG410XTFU. LUCA.
HOGENOMiHOG000131970.
InParanoidiQ74BP5.
OMAiCHKGKPR.
OrthoDBiPOG091H0RD1.

Family and domain databases

InterProiView protein in InterPro
IPR011031. Multihaem_cyt.
IPR026352. Nanowire_3heme.
SUPFAMiSSF48695. SSF48695. 2 hits.
TIGRFAMsiTIGR04257. nanowire_3heme. 4 hits.
PROSITEiView protein in PROSITE
PS51008. MULTIHEME_CYTC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q74BP5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMRLNGVVT GIVSLVLLVA VVAMAKETKN VPFKLKNAAP VIFSHDIHLK
60 70 80 90 100
KYNNNCRICH IALFDLRKPK RYTMLDMEKG KSCGACHTGM KAFSVADDSQ
110 120 130 140 150
CVRCHSGSAR PVAYRMKGAG EAVFSHEVHV PMLEGKCRTC HSNREITGGR
160 170 180 190 200
NVTMAQMEKG KSCGACHNDK MAFTVAGNCG KCHKGMTPPK TVNFKMKGVA
210 220 230 240 250
DAAFSHEFHL GMYKCNECHT KLFAYKAGAK RFTMADMDKG KSCGACHNGK
260 270 280 290 300
DAFSSASDCG KCHPGLKPAK LTYKTSVGEA YFDHDIHLSM FKCADCHTKV
310 320 330 340
FKYRKGSAPA TMADMEKGKS CGVCHNGKDA FSVADDCVKC HNM
Length:343
Mass (Da):37,451
Last modified:July 5, 2004 - v1
Checksum:iC038CDDEA9FEF619
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017180 Genomic DNA. Translation: AAR35372.1.
RefSeqiNP_953045.1. NC_002939.5.
WP_010942639.1. NC_002939.5.

Genome annotation databases

EnsemblBacteriaiAAR35372; AAR35372; GSU1996.
GeneIDi2686130.
KEGGigsu:GSU1996.
PATRICifig|243231.5.peg.2032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017180 Genomic DNA. Translation: AAR35372.1.
RefSeqiNP_953045.1. NC_002939.5.
WP_010942639.1. NC_002939.5.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RWJX-ray1.70A184-265[»]
3OUEX-ray2.15A186-343[»]
3OUQX-ray2.60A26-186[»]
3OV0X-ray3.20A26-343[»]
ProteinModelPortaliQ74BP5.
SMRiQ74BP5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243231.GSU1996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAR35372; AAR35372; GSU1996.
GeneIDi2686130.
KEGGigsu:GSU1996.
PATRICifig|243231.5.peg.2032.

Phylogenomic databases

eggNOGiENOG4105SNX. Bacteria.
ENOG410XTFU. LUCA.
HOGENOMiHOG000131970.
InParanoidiQ74BP5.
OMAiCHKGKPR.
OrthoDBiPOG091H0RD1.

Enzyme and pathway databases

BioCyciGSUL243231:GH27-2199-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ74BP5.

Family and domain databases

InterProiView protein in InterPro
IPR011031. Multihaem_cyt.
IPR026352. Nanowire_3heme.
SUPFAMiSSF48695. SSF48695. 2 hits.
TIGRFAMsiTIGR04257. nanowire_3heme. 4 hits.
PROSITEiView protein in PROSITE
PS51008. MULTIHEME_CYTC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ74BP5_GEOSL
AccessioniPrimary (citable) accession number: Q74BP5
Entry historyiIntegrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 7, 2017
This is version 83 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.