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Protein

Thioredoxin M-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 M form is known to activate NADP-malate dehydrogenase.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei98Deprotonates C-terminal active site Cys1
Active sitei104Nucleophile1
Sitei105Contributes to redox potential value1
Sitei106Contributes to redox potential value1
Active sitei107Nucleophile1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

SABIO-RKP07591.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin M-type, chloroplastic
Short name:
Trx-M
Cleaved into the following 2 chains:
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
Mutagenesisi107C → 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 – 67Chloroplast1 PublicationAdd BLAST67
ChainiPRO_000003417868 – 181Thioredoxin M-type, chloroplasticAdd BLAST114
ChainiPRO_000004589169 – 181Thioredoxin M-type McAdd BLAST113
ChainiPRO_000004589270 – 181Thioredoxin M-type MdAdd BLAST112

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi104 ↔ 107Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP07591.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ftrCQ553893EBI-537449,EBI-863211From a different organism.
PRXQQ9LU862EBI-537449,EBI-540311From a different organism.

Protein-protein interaction databases

DIPiDIP-33500N.
IntActiP07591. 43 interactors.

Structurei

Secondary structure

1181
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni81 – 83Combined sources3
Helixi84 – 87Combined sources4
Turni88 – 90Combined sources3
Beta strandi91 – 93Combined sources3
Beta strandi95 – 100Combined sources6
Helixi102 – 104Combined sources3
Helixi105 – 120Combined sources16
Turni121 – 124Combined sources4
Beta strandi126 – 131Combined sources6
Turni132 – 134Combined sources3
Helixi136 – 141Combined sources6
Beta strandi146 – 154Combined sources9
Beta strandi157 – 164Combined sources8
Helixi168 – 178Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FB0X-ray2.26A/B75-179[»]
1FB6X-ray2.10A/B75-179[»]
1GL8NMR-A76-179[»]
2PUKX-ray3.00C/G75-180[»]
ProteinModelPortaliP07591.
SMRiP07591.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07591.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 180ThioredoxinPROSITE-ProRule annotationAdd BLAST113

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.
TIGRFAMsiTIGR01068. thioredoxin. 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.

P07591-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIENCLQLS TSASVGTVAV KSHVHHLQPS SKVNVPTFRG LKRSFPALSS
60 70 80 90 100
SVSSSSPRQF RYSSVVCKAS EAVKEVQDVN DSSWKEFVLE SEVPVMVDFW
110 120 130 140 150
APWCGPCKLI APVIDELAKE YSGKIAVYKL NTDEAPGIAT QYNIRSIPTV
160 170 180
LFFKNGERKE SIIGAVPKST LTDSIEKYLS P
Length:181
Mass (Da):19,840
Last modified:November 1, 1997 - v2
Checksum:i5127D4BDF72D81E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti83S → G AA sequence (PubMed:3510868).Curated1
Sequence conflicti90 – 95ESEVPV → QSSEPS AA sequence (PubMed:3510868).Curated6
Sequence conflicti128Y → T AA sequence (PubMed:3510868).Curated1
Sequence conflicti165 – 170AVPKST → DVSKYQ AA sequence (PubMed:3510868).Curated6

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti25H → Y.1
Natural varianti33V → L.1
Natural varianti37T → S.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51462 mRNA. Translation: CAA35826.1.
X51463 mRNA. Translation: CAA35827.1.
PIRiS20496. TXSPM.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51462 mRNA. Translation: CAA35826.1.
X51463 mRNA. Translation: CAA35827.1.
PIRiS20496. TXSPM.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FB0X-ray2.26A/B75-179[»]
1FB6X-ray2.10A/B75-179[»]
1GL8NMR-A76-179[»]
2PUKX-ray3.00C/G75-180[»]
ProteinModelPortaliP07591.
SMRiP07591.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-33500N.
IntActiP07591. 43 interactors.

Proteomic databases

PRIDEiP07591.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP07591.

Miscellaneous databases

EvolutionaryTraceiP07591.

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.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXM_SPIOL
AccessioniPrimary (citable) accession number: P07591
Secondary accession number(s): Q41394, Q41395
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 117 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.