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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei98 – 981Deprotonates C-terminal active site Cys
Active sitei104 – 1041Nucleophile
Sitei105 – 1051Contributes to redox potential value
Sitei106 – 1061Contributes to redox potential value
Active sitei107 – 1071Nucleophile

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071C → S: Prevents scission of the intermolecular disulfide bond by the second Cys of the active site. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767Chloroplast1 PublicationAdd
BLAST
Chaini68 – 181114Thioredoxin M-type, chloroplasticPRO_0000034178Add
BLAST
Chaini69 – 181113Thioredoxin M-type McPRO_0000045891Add
BLAST
Chaini70 – 181112Thioredoxin M-type MdPRO_0000045892Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 107Redox-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
ftrCQ553893EBI-537449,EBI-863211From a different organism.
PRXQQ9LU862EBI-537449,EBI-540311From a different organism.

Protein-protein interaction databases

DIPiDIP-33500N.
IntActiP07591. 43 interactions.

Structurei

Secondary structure

1
181
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni81 – 833Combined sources
Helixi84 – 874Combined sources
Turni88 – 903Combined sources
Beta strandi91 – 933Combined sources
Beta strandi95 – 1006Combined sources
Helixi102 – 1043Combined sources
Helixi105 – 12016Combined sources
Turni121 – 1244Combined sources
Beta strandi126 – 1316Combined sources
Turni132 – 1343Combined sources
Helixi136 – 1416Combined sources
Beta strandi146 – 1549Combined sources
Beta strandi157 – 1648Combined sources
Helixi168 – 17811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FB0X-ray2.26A/B75-179[»]
1FB6X-ray2.10A/B75-179[»]
1GL8NMR-A76-179[»]
2PUKX-ray3.00C/G75-180[»]
ProteinModelPortaliP07591.
SMRiP07591. Positions 75-179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07591.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 180113ThioredoxinPROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831S → G AA sequence (PubMed:3510868).Curated
Sequence conflicti90 – 956ESEVPV → QSSEPS AA sequence (PubMed:3510868).Curated
Sequence conflicti128 – 1281Y → T AA sequence (PubMed:3510868).Curated
Sequence conflicti165 – 1706AVPKST → DVSKYQ AA sequence (PubMed:3510868).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251H → Y.
Natural varianti33 – 331V → L.
Natural varianti37 – 371T → S.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1FB0X-ray2.26A/B75-179[»]
1FB6X-ray2.10A/B75-179[»]
1GL8NMR-A76-179[»]
2PUKX-ray3.00C/G75-180[»]
ProteinModelPortaliP07591.
SMRiP07591. Positions 75-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-33500N.
IntActiP07591. 43 interactions.

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...

Publicationsi

  1. "Nucleotide sequence of cDNAs encoding the entire precursor polypeptide for thioredoxin m from spinach chloroplasts."
    Wedel N., Clausmeyer S., Herrmann R.G., Gardet-Salvi L., Schurmann P.
    Plant Mol. Biol. 18:527-533(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Further characterization and amino acid sequence of m-type thioredoxins from spinach chloroplasts."
    Maeda K., Tsugita A., Dalzoppo D., Vilbois F., Schurmann P.
    Eur. J. Biochem. 154:197-203(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 68-181.
  3. "Crystal structures of two functionally different thioredoxins in spinach chloroplasts."
    Capitani G., Markovic-Housley Z., DelVal G., Morris M., Jansonius J.N., Schurmann P.
    J. Mol. Biol. 302:135-154(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 75-179, DISULFIDE BOND.
  4. "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 (3.00 ANGSTROMS) OF 75-180 OF MUTANT SER-107 IN COMPLEXES WITH BACTERIAL FTRC; FTRV AND PETF/FERREDOXIN, SUBUNIT, MUTAGENESIS OF CYS-107.

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 11, 2015
This is version 114 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.