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Protein

Ferredoxin-thioredoxin reductase, catalytic chain

Gene

ftrC

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.4 Publications

Catalytic activityi

2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+.4 Publications

Cofactori

[4Fe-4S] cluster6 PublicationsNote: Binds 1 [4Fe-4S] cluster.6 Publications

Redox potential

E0 is -320 mV.1 Publication

Manual assertion based on experiment ini

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Iron-sulfur (4Fe-4S)2 Publications1
Active sitei58Nucleophile4 Publications1
Metal bindingi75Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi77Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi86Iron-sulfur (4Fe-4S)2 Publications1
Sitei87Increases the nucleophilicity of the active site Cys1 Publication1

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB
  • electron carrier activity Source: UniProtKB
  • ferredoxin:thioredoxin reductase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • oxidation-reduction process Source: UniProtKB
  • photosynthesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14463.

Names & Taxonomyi

Protein namesi
Recommended name:
Ferredoxin-thioredoxin reductase, catalytic chain4 PublicationsImported (EC:1.8.7.21 Publication)
Short name:
FTR-C4 Publications
Alternative name(s):
Ferredoxin-thioredoxin reductase subunit BBy similarity
Short name:
FTR-BBy similarity
Gene namesi
Name:ftrC1 PublicationImported
ORF Names:sll0554
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesMerismopediaceaeSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi58C → S: Loss of enzyme activity. 1 Publication1
Mutagenesisi87H → Y: Greatly reduced catalytic activity. Abolishes significant electronic interaction between the disulfide and a unique Fe site of the [4Fe-4S](2+) cluster in oxidized form of the reductase. 2 Publications1
Mutagenesisi88C → A: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004239261 – 118Ferredoxin-thioredoxin reductase, catalytic chainAdd BLAST118

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 88Redox-active2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ55389.

Expressioni

Inductioni

Dependent on photosynthetic conditions. Expression declines about 80-90% in the darkness. Re-illumination up-regulates the expression to normal levels. In the presence of glucose, expression is down-regulated by about 20%.1 Publication

Interactioni

Subunit structurei

Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit). Heterodimeric FTR forms a complex with ferredoxin and thioredoxin.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P075913EBI-863211,EBI-537449From a different organism.
P098564EBI-863211,EBI-863615From a different organism.
petFP273202EBI-863211,EBI-863421

Protein-protein interaction databases

DIPiDIP-35307N.
IntActiQ55389. 10 interactors.

Structurei

Secondary structure

1118
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 25Combined sources17
Beta strandi31 – 33Combined sources3
Helixi34 – 51Combined sources18
Beta strandi57 – 59Combined sources3
Helixi64 – 70Combined sources7
Beta strandi74 – 76Combined sources3
Helixi78 – 83Combined sources6
Beta strandi89 – 92Combined sources4
Beta strandi96 – 99Combined sources4
Helixi107 – 115Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJ7X-ray1.60A2-118[»]
2PU9X-ray1.65A9-118[»]
2PUKX-ray3.00A/E9-116[»]
2PUOX-ray1.70A8-116[»]
2PVDX-ray1.95A12-118[»]
2PVGX-ray2.40A11-116[»]
2PVOX-ray3.40A9-118[»]
ProteinModelPortaliQ55389.
SMRiQ55389.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55389.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

HOGENOMiHOG000265597.
InParanoidiQ55389.
KOiK17892.
OMAiDFAGKDQ.
PhylomeDBiQ55389.

Family and domain databases

Gene3Di3.90.460.10. 1 hit.
InterProiIPR024707. FTR_bsu_Cyano.
IPR004209. FTR_bsu_dom.
[Graphical view]
PfamiPF02943. FeThRed_B. 1 hit.
[Graphical view]
PIRSFiPIRSF000260. FTRc. 1 hit.
SUPFAMiSSF57662. SSF57662. 1 hit.

Sequencei

Sequence statusi: Complete.

Q55389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSSDTQNNK TLAAMKNFAE QYAKRTDTYF CSDLSVTAVV IEGLARHKEE
60 70 80 90 100
LGSPLCPCRH YEDKEAEVKN TFWNCPCVPM RERKECHCML FLTPDNDFAG
110
DAQDIPMETL EEVKASMA
Length:118
Mass (Da):13,390
Last modified:November 1, 1996 - v1
Checksum:i93B2F674C59A3CCE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10479.1.
PIRiS75744.

Genome annotation databases

EnsemblBacteriaiBAA10479; BAA10479; BAA10479.
KEGGisyn:sll0554.
PATRICi23842512. VBISynSp132158_2795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000022 Genomic DNA. Translation: BAA10479.1.
PIRiS75744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJ7X-ray1.60A2-118[»]
2PU9X-ray1.65A9-118[»]
2PUKX-ray3.00A/E9-116[»]
2PUOX-ray1.70A8-116[»]
2PVDX-ray1.95A12-118[»]
2PVGX-ray2.40A11-116[»]
2PVOX-ray3.40A9-118[»]
ProteinModelPortaliQ55389.
SMRiQ55389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35307N.
IntActiQ55389. 10 interactors.

Proteomic databases

PRIDEiQ55389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA10479; BAA10479; BAA10479.
KEGGisyn:sll0554.
PATRICi23842512. VBISynSp132158_2795.

Phylogenomic databases

HOGENOMiHOG000265597.
InParanoidiQ55389.
KOiK17892.
OMAiDFAGKDQ.
PhylomeDBiQ55389.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14463.

Miscellaneous databases

EvolutionaryTraceiQ55389.

Family and domain databases

Gene3Di3.90.460.10. 1 hit.
InterProiIPR024707. FTR_bsu_Cyano.
IPR004209. FTR_bsu_dom.
[Graphical view]
PfamiPF02943. FeThRed_B. 1 hit.
[Graphical view]
PIRSFiPIRSF000260. FTRc. 1 hit.
SUPFAMiSSF57662. SSF57662. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFTRC_SYNY3
AccessioniPrimary (citable) accession number: Q55389
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 105 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
  3. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

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.