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P80028

- TRXH_CHLRE

UniProt

P80028 - TRXH_CHLRE

Protein

Thioredoxin H-type

Gene

TRXH

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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. enzyme activator activity Source: EnsemblPlants/Gramene
    2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: EnsemblPlants/Gramene
    3. protein disulfide isomerase activity Source: EnsemblPlants/Gramene
    4. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell communication Source: EnsemblPlants/Gramene
    2. cell redox homeostasis Source: InterPro
    3. defense response to fungus Source: EnsemblPlants/Gramene
    4. glycerol ether metabolic process Source: InterPro
    5. heat acclimation Source: EnsemblPlants/Gramene
    6. protein oligomerization Source: EnsemblPlants/Gramene
    7. response to cadmium ion Source: EnsemblPlants/Gramene
    8. response to hydrogen peroxide Source: EnsemblPlants/Gramene
    9. response to microbial phytotoxin Source: EnsemblPlants/Gramene

    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. apoplast Source: EnsemblPlants/Gramene
    2. cell wall Source: EnsemblPlants/Gramene
    3. chloroplast stroma Source: EnsemblPlants/Gramene
    4. cytosol Source: EnsemblPlants/Gramene
    5. Golgi apparatus Source: EnsemblPlants/Gramene
    6. mitochondrion Source: EnsemblPlants/Gramene
    7. nucleus Source: EnsemblPlants/Gramene
    8. plasma membrane Source: EnsemblPlants/Gramene
    9. plasmodesma Source: EnsemblPlants/Gramene
    10. vacuole Source: EnsemblPlants/Gramene

    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 – 85
    Helixi11 – 2414
    Beta strandi28 – 336
    Beta strandi35 – 373
    Helixi38 – 5316
    Turni54 – 574
    Beta strandi58 – 647
    Turni65 – 684
    Helixi69 – 757
    Beta strandi79 – 879
    Beta strandi90 – 978
    Helixi100 – 11112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MGGSVIVIDS KAAWDAQLAK GKEEHKPIVV DFTATWCGPC KMIAPLFETL    50
    SNDYAGKVIF LKVDVDAVAA VAEAAGITAM PTFHVYKDGV KADDLVGASQ 100
    DKLKALVAKH AAA 113
    Length:113
    Mass (Da):11,844
    Last modified:January 23, 2007 - v3
    Checksum:iBCDDDCFA7810D3EE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 105 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