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Protein

Vitamin K epoxide reductase homolog

Gene

CYB_2278

Organism
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Thiol-disulfide oxidoreductase that catalyzes vitamin K-dependent disulfide bond formation in periplasmic target proteins.2 Publications

Enzyme regulationi

Inhibited by ferulenol.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei50Important for the reduction of the redox-active Cys-130 and Cys-1331
Sitei56Important for the reduction of the redox-active Cys-130 and Cys-1331
Sitei209Important for the reduction of the redox-active Cys-130 and Cys-1331
Sitei212Important for the reduction of the redox-active Cys-130 and Cys-1331

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciSSP321332:GH1B-2258-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K epoxide reductase homolog (EC:1.1.4.-)
Short name:
VKOR
Gene namesi
Ordered Locus Names:CYB_2278
OrganismiSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime)
Taxonomic identifieri321332 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeSynechococcus
Proteomesi
  • UP000001938 Componenti: Chromosome

Subcellular locationi

  • Membrane 2 Publications; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 20CytoplasmicAdd BLAST20
Transmembranei21 – 41HelicalAdd BLAST21
Topological domaini42 – 66PeriplasmicAdd BLAST25
Transmembranei67 – 87HelicalAdd BLAST21
Topological domaini88 – 102CytoplasmicAdd BLAST15
Transmembranei103 – 123HelicalAdd BLAST21
Topological domaini124 – 128Periplasmic5
Transmembranei129 – 149HelicalAdd BLAST21
Topological domaini150 – 158Cytoplasmic9
Transmembranei159 – 179HelicalAdd BLAST21
Topological domaini180 – 283PeriplasmicAdd BLAST104

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi41K → A: Reduces enzyme activity by about 40% with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi41K → E: Reduces enzyme activity by about 20% with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi41K → R: Minor effect on enzyme activity with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi41K → S: Reduces enzyme activity by about 75% with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi50C → A: Abolishes enzyme activity, but not with dithiothreitol as in vitro reductant. 2 Publications1
Mutagenesisi56C → A: Abolishes enzyme activity, but not with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi60L → A or G: Reduces enzyme activity. 1 Publication1
Mutagenesisi130C → A or S: Abolishes enzyme activity, also with dithiothreitol as in vitro reductant. 2 Publications1
Mutagenesisi133C → A: Abolishes enzyme activity, also with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi209C → A: Abolishes enzyme activity, but not with dithiothreitol as in vitro reductant. 1 Publication1
Mutagenesisi212C → A: Abolishes enzyme activity, but not with dithiothreitol as in vitro reductant. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004292651 – 283Vitamin K epoxide reductase homologAdd BLAST283

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50 ↔ 56Redox-active1 Publication
Disulfide bondi130 ↔ 133Redox-active1 Publication
Disulfide bondi209 ↔ 212Redox-active1 Publication
Disulfide bondi231 ↔ 2441 Publication

Keywords - PTMi

Disulfide bond, Quinone

Interactioni

Protein-protein interaction databases

STRINGi321332.CYB_2278.

Structurei

Secondary structure

1283
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 42Combined sources22
Helixi56 – 61Combined sources6
Beta strandi65 – 67Combined sources3
Helixi72 – 88Combined sources17
Helixi96 – 124Combined sources29
Helixi131 – 148Combined sources18
Beta strandi149 – 151Combined sources3
Helixi157 – 181Combined sources25
Helixi187 – 199Combined sources13
Beta strandi202 – 205Combined sources4
Helixi210 – 219Combined sources10
Helixi220 – 225Combined sources6
Beta strandi228 – 231Combined sources4
Helixi242 – 246Combined sources5
Beta strandi251 – 257Combined sources7
Beta strandi260 – 264Combined sources5
Helixi268 – 275Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KP8X-ray1.66A186-283[»]
3KP9X-ray3.60A1-283[»]
4NV2X-ray3.61A1-283[»]
4NV5X-ray2.79A/B1-283[»]
4NV6X-ray4.19A1-283[»]
ProteinModelPortaliQ2JJF6.
SMRiQ2JJF6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2JJF6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni59 – 65Quinone binding7
Regioni111 – 122Quinone bindingAdd BLAST12
Regioni186 – 283Thioredoxin-like domainAdd BLAST98

Domaini

Cysteine residues from the thioredoxin-like domain participate in a series of disulfide-exchange reactions that regenerate the redox-active cysteine residues in the transmembrane domain.

Sequence similaritiesi

Belongs to the VKOR family.Curated

Keywords - Domaini

Redox-active center, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CVB. Bacteria.
COG4243. LUCA.
HOGENOMiHOG000232446.
OMAiFSGYLMY.
OrthoDBiPOG091H084P.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR012932. VKOR.
[Graphical view]
PfamiPF07884. VKOR. 1 hit.
[Graphical view]
SMARTiSM00756. VKc. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Q2JJF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASYLKLKAQ EETWLQRHSR LILAILAGLG SLLTAYLTYT KLTEQPAAFC
60 70 80 90 100
TGDGGCDLVL SSRWAEFLGI PTAAVGLLGF LGVLALAVLP DGLPLVKRWR
110 120 130 140 150
WPALFGLVSA MTAFEMYMLY LMVAVLRQFC MYCTTAIILV AGLGLVTVLG
160 170 180 190 200
HRWLDGGKLA FSYILVAFLT LVTTIGVYAN QVPPPSPLAV GLAAHLRQIG
210 220 230 240 250
GTMYGAYWCP HCQDQKELFG AAFDQVPYVE CSPNGPGTPQ AQECTEAGIT
260 270 280
SYPTWIINGR TYTGVRSLEA LAVASGYPLE EGR
Length:283
Mass (Da):30,593
Last modified:March 7, 2006 - v1
Checksum:i615561731469DF16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000240 Genomic DNA. Translation: ABD03218.1.
RefSeqiWP_011433847.1. NC_007776.1.

Genome annotation databases

EnsemblBacteriaiABD03218; ABD03218; CYB_2278.
KEGGicyb:CYB_2278.
PATRICi23806900. VBISynSp29577_2279.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000240 Genomic DNA. Translation: ABD03218.1.
RefSeqiWP_011433847.1. NC_007776.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KP8X-ray1.66A186-283[»]
3KP9X-ray3.60A1-283[»]
4NV2X-ray3.61A1-283[»]
4NV5X-ray2.79A/B1-283[»]
4NV6X-ray4.19A1-283[»]
ProteinModelPortaliQ2JJF6.
SMRiQ2JJF6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi321332.CYB_2278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD03218; ABD03218; CYB_2278.
KEGGicyb:CYB_2278.
PATRICi23806900. VBISynSp29577_2279.

Phylogenomic databases

eggNOGiENOG4105CVB. Bacteria.
COG4243. LUCA.
HOGENOMiHOG000232446.
OMAiFSGYLMY.
OrthoDBiPOG091H084P.

Enzyme and pathway databases

BioCyciSSP321332:GH1B-2258-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ2JJF6.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR012932. VKOR.
[Graphical view]
PfamiPF07884. VKOR. 1 hit.
[Graphical view]
SMARTiSM00756. VKc. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVKOR_SYNJB
AccessioniPrimary (citable) accession number: Q2JJF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 11, 2014
Last sequence update: March 7, 2006
Last modified: November 2, 2016
This is version 66 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.