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Protein

Thioredoxin H-type

Gene

TRXH

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 4 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 H form is known to activate a number of cytosolic enzymes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei31 – 311Deprotonates C-terminal active site Cys
Active sitei37 – 371Nucleophile
Sitei38 – 381Contributes to redox potential value
Sitei39 – 391Contributes to redox potential value
Active sitei40 – 401Nucleophile

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H-type
Short name:
Trx-H
Alternative name(s):
Thioredoxin-CH1
Gene namesi
Name:TRXH
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 113112Thioredoxin H-typePRO_0000120055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 40Redox-activePROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP80028.
PRIDEiP80028.
ProMEXiP80028.

Interactioni

Protein-protein interaction databases

STRINGi3055.EDP02569.

Structurei

Secondary structure

1
113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi11 – 2414Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Helixi38 – 5316Combined sources
Turni54 – 574Combined sources
Beta strandi58 – 647Combined sources
Turni65 – 684Combined sources
Helixi69 – 757Combined sources
Beta strandi79 – 879Combined sources
Beta strandi90 – 978Combined sources
Helixi100 – 11112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EP7X-ray2.10A/B2-113[»]
1EP8X-ray2.20A/B2-113[»]
1TOFNMR-A2-113[»]
ProteinModelPortaliP80028.
SMRiP80028. Positions 2-113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80028.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 112111ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
KOiK03671.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
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.

P80028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGSVIVIDS KAAWDAQLAK GKEEHKPIVV DFTATWCGPC KMIAPLFETL
60 70 80 90 100
SNDYAGKVIF LKVDVDAVAA VAEAAGITAM PTFHVYKDGV KADDLVGASQ
110
DKLKALVAKH AAA
Length:113
Mass (Da):11,844
Last modified:January 23, 2007 - v3
Checksum:iBCDDDCFA7810D3EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78822 mRNA. Translation: CAA55399.1.
X80887 Genomic DNA. Translation: CAA56850.1.
PIRiS57775.
RefSeqiXP_001694574.1. XM_001694522.1.
UniGeneiCre.13338.

Genome annotation databases

EnsemblPlantsiEDP02569; EDP02569; CHLREDRAFT_195887.
GeneIDi5720085.
GrameneiEDP02569; EDP02569; CHLREDRAFT_195887.
KEGGicre:CHLREDRAFT_195887.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78822 mRNA. Translation: CAA55399.1.
X80887 Genomic DNA. Translation: CAA56850.1.
PIRiS57775.
RefSeqiXP_001694574.1. XM_001694522.1.
UniGeneiCre.13338.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EP7X-ray2.10A/B2-113[»]
1EP8X-ray2.20A/B2-113[»]
1TOFNMR-A2-113[»]
ProteinModelPortaliP80028.
SMRiP80028. Positions 2-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP02569.

Proteomic databases

PaxDbiP80028.
PRIDEiP80028.
ProMEXiP80028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDP02569; EDP02569; CHLREDRAFT_195887.
GeneIDi5720085.
GrameneiEDP02569; EDP02569; CHLREDRAFT_195887.
KEGGicre:CHLREDRAFT_195887.

Phylogenomic databases

eggNOGiKOG0907. Eukaryota.
COG0526. LUCA.
KOiK03671.

Miscellaneous databases

EvolutionaryTraceiP80028.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
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 nameiTRXH_CHLRE
AccessioniPrimary (citable) accession number: P80028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2007
Last modified: February 17, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

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.