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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi56 – 561Iron-sulfur (4Fe-4S)2 Publications
Active sitei58 – 581Nucleophile4 Publications
Metal bindingi75 – 751Iron-sulfur (4Fe-4S)2 Publications
Metal bindingi77 – 771Iron-sulfur (4Fe-4S)2 Publications
Metal bindingi86 – 861Iron-sulfur (4Fe-4S)2 Publications
Sitei87 – 871Increases the nucleophilicity of the active site Cys1 Publication

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 lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 581C → S: Loss of enzyme activity. 1 Publication
Mutagenesisi87 – 871H → 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 Publications
Mutagenesisi88 – 881C → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 118118Ferredoxin-thioredoxin reductase, catalytic chainPRO_0000423926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 88Redox-active2 Publications

Keywords - PTMi

Disulfide bond

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 interactions.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 2517Combined sources
Beta strandi31 – 333Combined sources
Helixi34 – 5118Combined sources
Beta strandi57 – 593Combined sources
Helixi64 – 707Combined sources
Beta strandi74 – 763Combined sources
Helixi78 – 836Combined sources
Beta strandi89 – 924Combined sources
Beta strandi96 – 994Combined sources
Helixi107 – 1159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 9-118.
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
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. Positions 9-118.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35307N.
IntActiQ55389. 10 interactions.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
    Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.
    , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  2. "Characterization of ferredoxin:thioredoxin reductase modified by site-directed mutagenesis."
    Glauser D.A., Bourquin F., Manieri W., Schurmann P.
    J. Biol. Chem. 279:16662-16669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF CYS-58; HIS-87 AND CYS-88.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  3. "Ferredoxin/ferredoxin-thioredoxin reductase complex: Complete NMR mapping of the interaction site on ferredoxin by gallium substitution."
    Xu X., Kim S.K., Schurmann P., Hirasawa M., Tripathy J.N., Smith J., Knaff D.B., Ubbink M.
    FEBS Lett. 580:6714-6720(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, SUBUNIT, NMR SPECTROSCOPY OF THE COMPLEX CONTAINING THE FTR HETERODIMER AND FERREDOXIN.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  4. "Role of histidine-86 in the catalytic mechanism of ferredoxin:thioredoxin reductase."
    Walters E.M., Garcia-Serres R., Naik S.G., Bourquin F., Glauser D.A., Schurmann P., Huynh B.H., Johnson M.K.
    Biochemistry 48:1016-1024(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, COFACTOR, EPR SPECTROSCOPY; RESONANCE RAMAN SPECTROSCOPY; MOSSBAUER SPECTROSCOPY AND MAGNETIC CIRCULAR DICHROISM, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-87.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  5. "Ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy."
    Xu X., Schurmann P., Chung J.S., Hass M.A., Kim S.K., Hirasawa M., Tripathy J.N., Knaff D.B., Ubbink M.
    J. Am. Chem. Soc. 131:17576-17582(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, NMR SPECTROSCOPY OF THE COMPLEX CONTAINING FERREDOXIN; THE FTR HETERODIMER AND TRX-M.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  6. "Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins."
    Perez-Perez M.E., Martin-Figueroa E., Florencio F.J.
    Mol. Plant 2:270-283(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  7. "Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster."
    Dai S., Schwendtmayer C., Schurmann P., Ramaswamy S., Eklund H.
    Science 287:655-658(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-118 IN COMPLEX WITH IRON-SULFUR (4FE-4S) AND FTRV, FUNCTION, COFACTOR, SUBUNIT, ACTIVE SITE, DISULFIDE BOND.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.
  8. "Structural snapshots along the reaction pathway of ferredoxin-thioredoxin reductase."
    Dai S., Friemann R., Glauser D.A., Bourquin F., Manieri W., Schurmann P., Eklund H.
    Nature 448:92-96(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 8-118 IN COMPLEXES WITH IRON-SULFUR (4FE-4S); FTRV; PETF/FERREDOXIN; TRX-F AND TRX-M, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, DISULFIDE BOND.
    Strain: ATCC 27184 / PCC 6803 / N-11 Publication.

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: March 16, 2016
This is version 103 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.