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P29448 (TRXH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thioredoxin H1

Short name=AtTrxh1
Alternative name(s):
Thioredoxin 1
Short name=AtTRX1
Gene names
Name:TRX1
Ordered Locus Names:At3g51030
ORF Names:F24M12.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the thioredoxin family. Plant H-type subfamily.

Contains 1 thioredoxin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 114114Thioredoxin H1
PRO_0000120046

Regions

Domain2 – 114113Thioredoxin

Sites

Active site401Nucleophile By similarity
Active site431Nucleophile By similarity
Site341Deprotonates C-terminal active site Cys By similarity
Site411Contributes to redox potential value By similarity
Site421Contributes to redox potential value By similarity

Amino acid modifications

Disulfide bond40 ↔ 43Redox-active Ref.8

Secondary structure

................... 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29448 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: E090761B2187F1F6

FASTA11412,673
        10         20         30         40         50         60 
MASEEGQVIA CHTVETWNEQ LQKANESKTL VVVDFTASWC GPCRFIAPFF ADLAKKLPNV 

        70         80         90        100        110 
LFLKVDTDEL KSVASDWAIQ AMPTFMFLKE GKILDKVVGA KKDELQSTIA KHLA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Solution structure of thioredoxin h1 from Arabidopsis thaliana."
Peterson F.C., Lytle B.L., Sampath S., Vinarov D., Tyler E., Shahan M., Markley J.L., Volkman B.F.
Protein Sci. 14:2195-2200(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJQ2242.
RefSeqNP_190672.1. NM_114963.4.
UniGeneAt.193.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XFLNMR-A1-114[»]
ProteinModelPortalP29448.
SMRP29448. Positions 1-114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP29448. 46 interactions.
STRING3702.AT3G51030.1-P.

Proteomic databases

PaxDbP29448.
PRIDEP29448.

Protocols and materials databases

DNASU824267.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G51030.1; AT3G51030.1; AT3G51030.
GeneID824267.
KEGGath:AT3G51030.

Organism-specific databases

TAIRAT3G51030.

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000292977.
InParanoidP29448.
KOK03671.
OMACRVISPI.
PhylomeDBP29448.

Gene expression databases

GenevestigatorP29448.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERPTHR10438. PTHR10438. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFPIRSF000077. Thioredoxin. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29448.

Entry information

Entry nameTRXH1_ARATH
AccessionPrimary (citable) accession number: P29448
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 11, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names