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P80028 (TRXH_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin H-type

Short name=Trx-H
Alternative name(s):
Thioredoxin-CH1
Gene names
Name:TRXH
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length113 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm.

Miscellaneous

This thioredoxin cannot be used as a substrate for E.coli NAPDH: thioredoxin reductase, but is a substrate of spinach ferredoxin-thioredoxin reductase and can activate NADP-MDH.

Sequence similarities

Belongs to the thioredoxin family. Plant H-type subfamily.

Contains 1 thioredoxin domain.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentCytoplasm
   DomainRedox-active center
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcell communication

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

defense response to fungus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

glycerol ether metabolic process

Inferred from electronic annotation. Source: InterPro

heat acclimation

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

protein oligomerization

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to hydrogen peroxide

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to microbial phytotoxin

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

apoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cell wall

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast stroma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

cytosol

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

mitochondrion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

nucleus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasma membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

vacuole

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functionenzyme activator activity

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

protein disulfide isomerase activity

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

protein disulfide oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 113112Thioredoxin H-type
PRO_0000120055

Regions

Domain2 – 112111Thioredoxin

Sites

Active site371Nucleophile
Active site401Nucleophile
Site311Deprotonates C-terminal active site Cys
Site381Contributes to redox potential value
Site391Contributes to redox potential value

Amino acid modifications

Disulfide bond37 ↔ 40Redox-active Ref.2

Secondary structure

.................... 113
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P80028 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BCDDDCFA7810D3EE

FASTA11311,844
        10         20         30         40         50         60 
MGGSVIVIDS KAAWDAQLAK GKEEHKPIVV DFTATWCGPC KMIAPLFETL SNDYAGKVIF 

        70         80         90        100        110 
LKVDVDAVAA VAEAAGITAM PTFHVYKDGV KADDLVGASQ DKLKALVAKH AAA 

« Hide

References

[1]"Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties."
Stein M., Jacquot J.-P., Jeannette E., Decottignies P., Hodges M., Lancelin J.-M., Mittard V., Schmitter J.-M., Miginiac-Maslow M.
Plant Mol. Biol. 28:487-503(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Characterization and primary structure of a second thioredoxin from the green alga, Chlamydomonas reinhardtii."
Decottignies P., Schmitter J.-M., Dutka S., Jacquot J.-P., Miginiac-Maslow M.
Eur. J. Biochem. 198:505-512(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-112, DISULFIDE BOND.
Strain: 137c / CC-125.
[3]"NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii."
Mittard V., Blackledge M.J., Stein M., Jacquot J.-P., Marion D., Lancelin J.-M.
Eur. J. Biochem. 243:374-383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism."
Menchise V., Corbier C., Didierjean C., Saviano M., Benedetti E., Jacquot J.-P., Aubry A.
Biochem. J. 359:65-75(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78822 mRNA. Translation: CAA55399.1.
X80887 Genomic DNA. Translation: CAA56850.1.
PIRS57775.
RefSeqXP_001694574.1. XM_001694522.1.
UniGeneCre.13338.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EP7X-ray2.10A/B2-113[»]
1EP8X-ray2.20A/B2-113[»]
1TOFNMR-A2-113[»]
ProteinModelPortalP80028.
SMRP80028. Positions 2-113.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP80028.
ProMEXP80028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5720085.
KEGGcre:CHLREDRAFT_195887.

Phylogenomic databases

eggNOGCOG0526.
KOK03671.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
PRINTSPR00421. THIOREDOXIN.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP80028.

Entry information

Entry nameTRXH_CHLRE
AccessionPrimary (citable) accession number: P80028
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references