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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi48 – 481Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Metal bindingi48 – 481Iron (heme 7 axial ligand); via tele nitrogenCombined sources
Binding sitei56 – 561Heme 1 (covalent)Combined sources
Binding sitei59 – 591Heme 1 (covalent)Combined sources
Metal bindingi60 – 601Iron (heme 1 axial ligand); via tele nitrogenCombined sources
Metal bindingi74 – 741Iron (heme 2 axial ligand)Combined sources
Metal bindingi74 – 741Iron (heme 4 axial ligand)Combined sources
Binding sitei83 – 831Heme 3 (covalent)Combined sources
Binding sitei83 – 831Heme 7 (covalent)Combined sources
Binding sitei86 – 861Heme 3 (covalent)Combined sources
Binding sitei86 – 861Heme 7 (covalent)Combined sources
Metal bindingi87 – 871Iron (heme 3 axial ligand); via tele nitrogenCombined sources
Metal bindingi87 – 871Iron (heme 7 axial ligand); via tele nitrogenCombined sources
Binding sitei101 – 1011Heme 2 (covalent)Combined sources
Binding sitei101 – 1011Heme 4 (covalent)Combined sources
Binding sitei104 – 1041Heme 2 (covalent)Combined sources
Binding sitei104 – 1041Heme 4 (covalent)Combined sources
Metal bindingi105 – 1051Iron (heme 2 axial ligand); via tele nitrogenCombined sources
Metal bindingi105 – 1051Iron (heme 4 axial ligand); via tele nitrogenCombined sources
Metal bindingi126 – 1261Iron (heme 5 axial ligand); via tele nitrogenCombined sources
Metal bindingi126 – 1261Iron (heme 6 axial ligand); via tele nitrogenCombined sources
Metal bindingi129 – 1291Iron (heme 10 axial ligand); via tele nitrogenCombined sources
Metal bindingi129 – 1291Iron (heme 11 axial ligand); via tele nitrogenCombined sources
Binding sitei137 – 1371Heme 5 (covalent)Combined sources
Binding sitei137 – 1371Heme 6 (covalent)Combined sources
Binding sitei140 – 1401Heme 5 (covalent)Combined sources
Binding sitei140 – 1401Heme 6 (covalent)Combined sources
Metal bindingi141 – 1411Iron (heme 5 axial ligand); via tele nitrogenCombined sources
Metal bindingi141 – 1411Iron (heme 6 axial ligand); via tele nitrogenCombined sources
Metal bindingi154 – 1541Iron (heme 8 axial ligand)Combined sources
Metal bindingi154 – 1541Iron (heme 9 axial ligand)Combined sources
Binding sitei163 – 1631Heme 10 (covalent)Combined sources
Binding sitei163 – 1631Heme 11 (covalent)Combined sources
Binding sitei166 – 1661Heme 10 (covalent)Combined sources
Binding sitei166 – 1661Heme 11 (covalent)Combined sources
Metal bindingi167 – 1671Iron (heme 10 axial ligand); via tele nitrogenCombined sources
Metal bindingi167 – 1671Iron (heme 11 axial ligand); via tele nitrogenCombined sources
Binding sitei179 – 1791Heme 8 (covalent)Combined sources
Binding sitei179 – 1791Heme 9 (covalent)Combined sources
Binding sitei182 – 1821Heme 8 (covalent)Combined sources
Binding sitei182 – 1821Heme 9 (covalent)Combined sources
Metal bindingi183 – 1831Iron (heme 8 axial ligand); via tele nitrogenCombined sources
Metal bindingi183 – 1831Iron (heme 9 axial ligand); via tele nitrogenCombined sources
Metal bindingi206 – 2061Iron (heme 12 axial ligand); via tele nitrogenCombined sources
Metal bindingi209 – 2091Iron (heme 14 axial ligand); via tele nitrogenCombined sources
Binding sitei215 – 2151Heme 12 (covalent)Combined sources
Binding sitei218 – 2181Heme 12 (covalent)Combined sources
Metal bindingi219 – 2191Iron (heme 12 axial ligand); via tele nitrogenCombined sources
Metal bindingi234 – 2341Iron (heme 13 axial ligand)Combined sources
Binding sitei243 – 2431Heme 14 (covalent)Combined sources
Binding sitei246 – 2461Heme 14 (covalent)Combined sources
Metal bindingi247 – 2471Iron (heme 14 axial ligand); via tele nitrogenCombined sources
Binding sitei259 – 2591Heme 13 (covalent)Combined sources
Binding sitei262 – 2621Heme 13 (covalent)Combined sources
Metal bindingi263 – 2631Iron (heme 13 axial ligand); via tele nitrogenCombined sources
Metal bindingi284 – 2841Iron (heme 15 axial ligand); via tele nitrogenCombined sources
Metal bindingi287 – 2871Iron (heme 17 axial ligand); via tele nitrogenCombined sources
Metal bindingi287 – 2871Iron (heme 18 axial ligand); via tele nitrogenCombined sources
Binding sitei293 – 2931Heme 15 (covalent)Combined sources
Binding sitei296 – 2961Heme 15 (covalent)Combined sources
Metal bindingi297 – 2971Iron (heme 15 axial ligand); via tele nitrogenCombined sources
Metal bindingi312 – 3121Iron (heme 16 axial ligand)Combined sources
Binding sitei321 – 3211Heme 17 (covalent)Combined sources
Binding sitei321 – 3211Heme 18 (covalent)Combined sources
Binding sitei324 – 3241Heme 17 (covalent)Combined sources
Binding sitei324 – 3241Heme 18 (covalent)Combined sources
Metal bindingi325 – 3251Iron (heme 17 axial ligand); via tele nitrogenCombined sources
Metal bindingi325 – 3251Iron (heme 18 axial ligand); via tele nitrogenCombined sources
Binding sitei337 – 3371Heme 16 (covalent)Combined sources
Binding sitei340 – 3401Heme 16 (covalent)Combined sources
Metal bindingi341 – 3411Iron (heme 16 axial ligand); via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

HemeCombined sources, Iron, Metal-binding

Enzyme and pathway databases

BioCyciGSUL243231:GH27-2026-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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RWJX-ray1.70A184-265[»]
3OUEX-ray2.15A186-343[»]
3OUQX-ray2.60A26-186[»]
3OV0X-ray3.20A26-343[»]
ProteinModelPortaliQ74BP5.
SMRiQ74BP5. Positions 184-264, 277-341.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ74BP5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 330280Cytochrome cInterPro annotationAdd
BLAST

Phylogenomic databases

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

Family and domain databases

InterProiIPR011031. Multihaem_cyt.
IPR026352. Nanowire_3heme.
[Graphical view]
SUPFAMiSSF48695. SSF48695. 2 hits.
TIGRFAMsiTIGR04257. nanowire_3heme. 4 hits.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]

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.
PATRICi22026853. VBIGeoSul17553_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
EntryMethodResolution (Å)ChainPositionsPDBsum
1RWJX-ray1.70A184-265[»]
3OUEX-ray2.15A186-343[»]
3OUQX-ray2.60A26-186[»]
3OV0X-ray3.20A26-343[»]
ProteinModelPortaliQ74BP5.
SMRiQ74BP5. Positions 184-264, 277-341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243231.GSU1996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAR35372; AAR35372; GSU1996.
GeneIDi2686130.
KEGGigsu:GSU1996.
PATRICi22026853. VBIGeoSul17553_2032.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciGSUL243231:GH27-2026-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ74BP5.

Family and domain databases

InterProiIPR011031. Multihaem_cyt.
IPR026352. Nanowire_3heme.
[Graphical view]
SUPFAMiSSF48695. SSF48695. 2 hits.
TIGRFAMsiTIGR04257. nanowire_3heme. 4 hits.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ74BP5_GEOSL
AccessioniPrimary (citable) accession number: Q74BP5
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 79 of the entry and version 1 of the sequence. [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.