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Protein

Thioredoxin F-type, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The F form is known to activate a number of enzymes of the photosynthetic carbon cycle.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei108Deprotonates C-terminal active site Cys1
Active sitei114Nucleophile1
Sitei115Contributes to redox potential value1
Sitei116Contributes to redox potential value1
Active sitei117Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

SABIO-RKP09856.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin F-type, chloroplastic
Short name:
Trx-F
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi117C → S: Prevents scission of the intermolecular disulfide bond by the second Cys of the active site. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 77Chloroplast1 PublicationAdd BLAST77
ChainiPRO_000003416178 – 190Thioredoxin F-type, chloroplasticAdd BLAST113

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi114 ↔ 117Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Forms a complex with heterodimeric ferredoxin-thioredoxin reductase (FTR) and ferredoxin.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ftrCQ553894EBI-863615,EBI-863211From a different organism.

Protein-protein interaction databases

DIPiDIP-37834N.
IntActiP09856. 1 interactor.

Structurei

Secondary structure

1190
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi75 – 79Combined sources5
Turni80 – 83Combined sources4
Beta strandi84 – 88Combined sources5
Turni90 – 92Combined sources3
Helixi93 – 97Combined sources5
Turni100 – 102Combined sources3
Beta strandi105 – 110Combined sources6
Helixi115 – 130Combined sources16
Beta strandi134 – 140Combined sources7
Beta strandi142 – 145Combined sources4
Helixi146 – 152Combined sources7
Beta strandi155 – 175Combined sources21
Helixi177 – 188Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F9MX-ray1.86A/B78-189[»]
1FAAX-ray1.85A69-189[»]
2PU9X-ray1.65C79-189[»]
2PVOX-ray3.40C79-189[»]
ProteinModelPortaliP09856.
SMRiP09856.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09856.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 189ThioredoxinPROSITE-ProRule annotationAdd BLAST112

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09856-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALHLSLSHQ SWTSPAHPIT SSDPTRSSVP GTGLSRRVDF LGSCKINGVF
60 70 80 90 100
VVKRKDRRRM RGGEVRASME QALGTQEMEA IVGKVTEVNK DTFWPIVKAA
110 120 130 140 150
GDKPVVLDMF TQWCGPCKAM APKYEKLAEE YLDVIFLKLD CNQENKTLAK
160 170 180 190
ELGIRVVPTF KILKENSVVG EVTGAKYDKL LEAIQAARSS
Length:190
Mass (Da):21,024
Last modified:October 1, 1989 - v2
Checksum:i4B162C69DBC11869
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14959 mRNA. Translation: CAA33082.1.
PIRiS04661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14959 mRNA. Translation: CAA33082.1.
PIRiS04661.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F9MX-ray1.86A/B78-189[»]
1FAAX-ray1.85A69-189[»]
2PU9X-ray1.65C79-189[»]
2PVOX-ray3.40C79-189[»]
ProteinModelPortaliP09856.
SMRiP09856.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37834N.
IntActiP09856. 1 interactor.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP09856.

Miscellaneous databases

EvolutionaryTraceiP09856.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXF_SPIOL
AccessioniPrimary (citable) accession number: P09856
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: November 2, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.