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Protein

Thioredoxin H1

Gene

TRX1

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 135Combined sources
Helixi14 – 2613Combined sources
Beta strandi30 – 367Combined sources
Helixi41 – 5616Combined sources
Beta strandi58 – 669Combined sources
Turni67 – 693Combined sources
Helixi71 – 766Combined sources
Beta strandi81 – 899Combined sources
Beta strandi92 – 998Combined sources
Helixi102 – 11211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiLTSANFE.
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

        10         20         30         40         50
MASEEGQVIA CHTVETWNEQ LQKANESKTL VVVDFTASWC GPCRFIAPFF
60 70 80 90 100
ADLAKKLPNV LFLKVDTDEL KSVASDWAIQ AMPTFMFLKE GKILDKVVGA
110
KKDELQSTIA KHLA
Length:114
Mass (Da):12,673
Last modified:April 1, 1993 - v1
Checksum:iE090761B2187F1F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP29448.
PRIDEiP29448.

Protocols and materials databases

DNASUi824267.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT3G51030.

Phylogenomic databases

eggNOGiCOG0526.
HOGENOMiHOG000292977.
InParanoidiP29448.
KOiK03671.
OMAiLTSANFE.
PhylomeDBiP29448.

Miscellaneous databases

EvolutionaryTraceiP29448.

Gene expression databases

GenevestigatoriP29448.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 123 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

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 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.