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P80028

- TRXH_CHLRE

UniProt

P80028 - TRXH_CHLRE

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Protein

Thioredoxin H-type

Gene

TRXH

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - 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 - Molecular functioni

  1. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. glycerol ether metabolic process Source: InterPro
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

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 113112Thioredoxin H-typePRO_0000120055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi37 ↔ 40Redox-active1 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP80028.
ProMEXiP80028.

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

eggNOGiCOG0526.
KOiK03671.

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]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
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

GeneIDi5720085.
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 .
PIRi S57775.
RefSeqi XP_001694574.1. XM_001694522.1.
UniGenei Cre.13338.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EP7 X-ray 2.10 A/B 2-113 [» ]
1EP8 X-ray 2.20 A/B 2-113 [» ]
1TOF NMR - A 2-113 [» ]
ProteinModelPortali P80028.
SMRi P80028. Positions 2-113.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P80028.
ProMEXi P80028.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5720085.
KEGGi cre:CHLREDRAFT_195887.

Phylogenomic databases

eggNOGi COG0526.
KOi K03671.

Miscellaneous databases

EvolutionaryTracei P80028.

Family and domain databases

Gene3Di 3.40.30.10. 1 hit.
InterProi IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view ]
PANTHERi PTHR10438. PTHR10438. 1 hit.
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
PIRSFi PIRSF000077. Thioredoxin. 1 hit.
SUPFAMi SSF52833. SSF52833. 1 hit.
PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

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: November 26, 2014
This is version 107 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

External Data

Dasty 3