Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nine-heme cytochrome c

Gene

Ddes_2038

Organism
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May form part of a transmembrane redox complex through which electrons are transferred to the cytoplasm for reduction of sulfate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Iron (heme 1 axial ligand)
Metal bindingi70 – 701Iron (heme 3 axial ligand)
Binding sitei77 – 771Heme 1 (covalent)
Binding sitei80 – 801Heme 1 (covalent)
Metal bindingi81 – 811Iron (heme 1 axial ligand)
Metal bindingi82 – 821Iron (heme 2 axial ligand)
Binding sitei89 – 891Heme 2 (covalent)
Binding sitei92 – 921Heme 2 (covalent)
Metal bindingi93 – 931Iron (heme 2 axial ligand)
Metal bindingi111 – 1111Iron (heme 5 axial ligand)
Binding sitei127 – 1271Heme 3 (covalent)
Binding sitei130 – 1301Heme 3 (covalent)
Metal bindingi131 – 1311Iron (heme 3 axial ligand)
Binding sitei141 – 1411Heme 4 (covalent)
Binding sitei144 – 1441Heme 4 (covalent)
Metal bindingi145 – 1451Iron (heme 4 axial ligand)
Binding sitei157 – 1571Heme 5 (covalent)
Binding sitei160 – 1601Heme 5 (covalent)
Metal bindingi161 – 1611Iron (heme 5 axial ligand)
Metal bindingi227 – 2271Iron (heme 6 axial ligand)
Metal bindingi230 – 2301Iron (heme 8 axial ligand)
Metal bindingi248 – 2481Iron (heme 4 axial ligand)
Binding sitei255 – 2551Heme 6 (covalent)
Binding sitei258 – 2581Heme 6 (covalent)
Metal bindingi259 – 2591Iron (heme 6 axial ligand)
Metal bindingi260 – 2601Iron (heme 7 axial ligand)
Binding sitei271 – 2711Heme 7 (covalent)
Binding sitei274 – 2741Heme 7 (covalent)
Metal bindingi275 – 2751Iron (heme 7 axial ligand)
Metal bindingi294 – 2941Iron (heme 9 axial ligand)
Binding sitei297 – 2971Heme 8 (covalent)
Binding sitei300 – 3001Heme 8 (covalent)
Metal bindingi301 – 3011Iron (heme 8 axial ligand)
Binding sitei314 – 3141Heme 9 (covalent)
Binding sitei317 – 3171Heme 9 (covalent)
Metal bindingi318 – 3181Iron (heme 9 axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciDDES525146:GIWF-2104-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nine-heme cytochrome c
Alternative name(s):
9Hcc
Gene namesi
Ordered Locus Names:Ddes_2038
OrganismiDesulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Taxonomic identifieri525146 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio
Proteomesi
  • UP000002598 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 – 3030Add
BLAST
Chaini31 – 326296Nine-heme cytochrome cPRO_0000006594Add
BLAST

Post-translational modificationi

Binds 9 heme groups per subunit.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi525146.Ddes_2038.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 404Combined sources
Beta strandi42 – 465Combined sources
Beta strandi63 – 664Combined sources
Helixi67 – 737Combined sources
Helixi77 – 804Combined sources
Helixi89 – 913Combined sources
Helixi99 – 1013Combined sources
Helixi106 – 1116Combined sources
Beta strandi119 – 1213Combined sources
Helixi127 – 13711Combined sources
Helixi139 – 1424Combined sources
Helixi144 – 1474Combined sources
Helixi154 – 1607Combined sources
Helixi169 – 1779Combined sources
Helixi182 – 19413Combined sources
Helixi204 – 2063Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi218 – 2203Combined sources
Beta strandi223 – 2253Combined sources
Helixi227 – 23610Combined sources
Turni237 – 2404Combined sources
Helixi242 – 2476Combined sources
Helixi253 – 2575Combined sources
Helixi271 – 2733Combined sources
Helixi289 – 30315Combined sources
Beta strandi314 – 3185Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
19HCX-ray1.80A/B31-321[»]
1OFWX-ray1.50A/B31-326[»]
1OFYX-ray2.00A/B31-326[»]
ProteinModelPortaliQ9RN68.
SMRiQ9RN68. Positions 31-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RN68.

Family & Domainsi

Domaini

Arranged into two tetraheme clusters and the extra heme 4 is located asymmetrically between the two regions.

Sequence similaritiesi

Contains 9 cytochrome c domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105F1C. Bacteria.
ENOG410XRT9. LUCA.
OrthoDBiPOG091H0RGX.

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 2 hits.
[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.

Q9RN68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNGTSLLLL AAIALAGAAC LTAMGGTAKA AALEPTDSGA PSAIVMFPVG
60 70 80 90 100
EKPNPKGAAM KPVVFNHLIH EKKIDNCETC HHTGDPVSCS TCHTVEGKAE
110 120 130 140 150
GNYITLDRAM HATNIAKRAK GNTPVSCVSC HEQQTKERRE CAGCHAIVTP
160 170 180 190 200
KRDEAWCATC HNITPSMTPE QMQKGINGTL LPGDNEALAA ETVLAQKTVE
210 220 230 240 250
PVSPMLAPYK VVIDALADKY EPSNFTHRRH LTSLMERIKD DKLAQAFHNK
260 270 280 290 300
PEILCATCHH RSPLSLTPPK CGSCHTKEID KANPGRPNLM AAYHLQCMGC
310 320
HKGMDVARPR DTDCTTCHKA APKSAD
Length:326
Mass (Da):35,025
Last modified:May 1, 2000 - v1
Checksum:i2ED7025ADDF250E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF186393 Genomic DNA. Translation: AAD56586.1.
CP001358 Genomic DNA. Translation: ACL49934.1.
PIRiJC7094.
RefSeqiWP_012625658.1. NC_011883.1.

Genome annotation databases

EnsemblBacteriaiACL49934; ACL49934; Ddes_2038.
KEGGidds:Ddes_2038.
PATRICi21738090. VBIDesDes50650_2377.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF186393 Genomic DNA. Translation: AAD56586.1.
CP001358 Genomic DNA. Translation: ACL49934.1.
PIRiJC7094.
RefSeqiWP_012625658.1. NC_011883.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
19HCX-ray1.80A/B31-321[»]
1OFWX-ray1.50A/B31-326[»]
1OFYX-ray2.00A/B31-326[»]
ProteinModelPortaliQ9RN68.
SMRiQ9RN68. Positions 31-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi525146.Ddes_2038.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL49934; ACL49934; Ddes_2038.
KEGGidds:Ddes_2038.
PATRICi21738090. VBIDesDes50650_2377.

Phylogenomic databases

eggNOGiENOG4105F1C. Bacteria.
ENOG410XRT9. LUCA.
OrthoDBiPOG091H0RGX.

Enzyme and pathway databases

BioCyciDDES525146:GIWF-2104-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9RN68.

Family and domain databases

InterProiIPR002322. Cyt_c_III.
IPR020942. Cyt_c_III_dom.
IPR011031. Multihaem_cyt.
[Graphical view]
PfamiPF02085. Cytochrom_CIII. 2 hits.
[Graphical view]
PRINTSiPR00609. CYTOCHROMEC3.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYC9_DESDA
AccessioniPrimary (citable) accession number: Q9RN68
Secondary accession number(s): B8J3C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 84 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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.