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P29448

- TRXH1_ARATH

UniProt

P29448 - TRXH1_ARATH

Protein

Thioredoxin H1

Gene

TRX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Thiol-disulfide oxidoreductase involved in the redox regulation of a number of cytosolic enzymes. Activates the cytosolic malate dehydrogenase (MDH) probably by reducing an interchain disulfid bond of the inactive MDH homodimer. Possesses insulin disulfide bonds reducing activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei34 – 341Deprotonates C-terminal active site CysBy similarity
    Active sitei40 – 401NucleophileBy similarity
    Sitei41 – 411Contributes to redox potential valueBy similarity
    Sitei42 – 421Contributes to redox potential valueBy similarity
    Active sitei43 – 431NucleophileBy similarity

    GO - Molecular functioni

    1. enzyme activator activity Source: UniProtKB
    2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: TAIR
    3. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glycerol ether metabolic process Source: InterPro
    3. positive regulation of catalytic activity Source: UniProtKB

    Keywords - Biological processi

    Electron transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin H1
    Short name:
    AtTrxh1
    Alternative name(s):
    Thioredoxin 1
    Short name:
    AtTRX1
    Gene namesi
    Name:TRX1
    Ordered Locus Names:At3g51030
    ORF Names:F24M12.70
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G51030.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. cytosol Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 114114Thioredoxin H1PRO_0000120046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 43Redox-active1 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP29448.
    PRIDEiP29448.

    Expressioni

    Gene expression databases

    GenevestigatoriP29448.

    Interactioni

    Protein-protein interaction databases

    IntActiP29448. 46 interactions.
    STRINGi3702.AT3G51030.1-P.

    Structurei

    Secondary structure

    1
    114
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 135
    Helixi14 – 2613
    Beta strandi30 – 367
    Helixi41 – 5616
    Beta strandi58 – 669
    Turni67 – 693
    Helixi71 – 766
    Beta strandi81 – 899
    Beta strandi92 – 998
    Helixi102 – 11211

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XFLNMR-A1-114[»]
    ProteinModelPortaliP29448.
    SMRiP29448. Positions 1-114.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29448.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 114113ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    HOGENOMiHOG000292977.
    InParanoidiP29448.
    KOiK03671.
    OMAiCRVISPI.
    PhylomeDBiP29448.

    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.

    P29448-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASEEGQVIA CHTVETWNEQ LQKANESKTL VVVDFTASWC GPCRFIAPFF    50
    ADLAKKLPNV LFLKVDTDEL KSVASDWAIQ AMPTFMFLKE GKILDKVVGA 100
    KKDELQSTIA KHLA 114
    Length:114
    Mass (Da):12,673
    Last modified:April 1, 1993 - v1
    Checksum:iE090761B2187F1F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14084 mRNA. Translation: CAA78462.1.
    U35827 Genomic DNA. Translation: AAC49354.1.
    AL132980 Genomic DNA. Translation: CAB62625.1.
    CP002686 Genomic DNA. Translation: AEE78739.1.
    AY088687 mRNA. Translation: AAM67008.1.
    PIRiJQ2242.
    RefSeqiNP_190672.1. NM_114963.4.
    UniGeneiAt.193.

    Genome annotation databases

    EnsemblPlantsiAT3G51030.1; AT3G51030.1; AT3G51030.
    GeneIDi824267.
    KEGGiath:AT3G51030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14084 mRNA. Translation: CAA78462.1 .
    U35827 Genomic DNA. Translation: AAC49354.1 .
    AL132980 Genomic DNA. Translation: CAB62625.1 .
    CP002686 Genomic DNA. Translation: AEE78739.1 .
    AY088687 mRNA. Translation: AAM67008.1 .
    PIRi JQ2242.
    RefSeqi NP_190672.1. NM_114963.4.
    UniGenei At.193.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XFL NMR - A 1-114 [» ]
    ProteinModelPortali P29448.
    SMRi P29448. Positions 1-114.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P29448. 46 interactions.
    STRINGi 3702.AT3G51030.1-P.

    Proteomic databases

    PaxDbi P29448.
    PRIDEi P29448.

    Protocols and materials databases

    DNASUi 824267.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G51030.1 ; AT3G51030.1 ; AT3G51030 .
    GeneIDi 824267.
    KEGGi ath:AT3G51030.

    Organism-specific databases

    TAIRi AT3G51030.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000292977.
    InParanoidi P29448.
    KOi K03671.
    OMAi CRVISPI.
    PhylomeDBi P29448.

    Miscellaneous databases

    EvolutionaryTracei P29448.

    Gene expression databases

    Genevestigatori P29448.

    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. "Nucleotide sequence of a cDNA clone encoding an Arabidopsis thaliana thioredoxin h."
      Rivera-Madrid R., Marinho P., Brugidou C., Chartier Y., Meyer Y.
      Plant Physiol. 102:327-328(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Intron position as an evolutionary marker of thioredoxins and thioredoxin domains."
      Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.
      J. Mol. Evol. 42:422-431(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Landsberg erecta.
    3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Thioredoxin-h1 reduces and reactivates the oxidized cytosolic malate dehydrogenase dimer in higher plants."
      Hara S., Motohashi K., Arisaka F., Romano P.G., Hosoya-Matsuda N., Kikuchi N., Fusada N., Hisabori T.
      J. Biol. Chem. 281:32065-32071(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Comparative genomic study of the thioredoxin family in photosynthetic organisms with emphasis on Populus trichocarpa."
      Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.
      Mol. Plant 2:308-322(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    8. Cited for: STRUCTURE BY NMR, DISULFIDE BOND.

    Entry informationi

    Entry nameiTRXH1_ARATH
    AccessioniPrimary (citable) accession number: P29448
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3