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Protein

Thioredoxin H-type

Gene
N/A
Organism
Populus jackii (Balm of Gilead) (Populus deltoides x Populus balsamifera)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei58NucleophileBy similarity1
Sitei59Contributes to redox potential valueBy similarity1
Sitei60Contributes to redox potential valueBy similarity1
Active sitei61NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin H-type
Alternative name(s):
Trxh4
OrganismiPopulus jackii (Balm of Gilead) (Populus deltoides x Populus balsamifera)
Taxonomic identifieri640484 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00003414852 – 139Thioredoxin H-type1 PublicationAdd BLAST138

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 61Redox-activePROSITE-ProRule annotationBy similarity

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1139
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 29Combined sources3
Helixi32 – 45Combined sources14
Beta strandi49 – 54Combined sources6
Helixi59 – 74Combined sources16
Beta strandi78 – 84Combined sources7
Turni85 – 87Combined sources3
Helixi89 – 94Combined sources6
Beta strandi99 – 107Combined sources9
Beta strandi110 – 117Combined sources8
Helixi120 – 132Combined sources13
Turni136 – 138Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D21X-ray2.15A/B1-139[»]
3D22X-ray1.60A1-139[»]
ProteinModelPortaliP85801.
SMRiP85801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP85801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 132ThioredoxinPROSITE-ProRule annotationAdd BLAST113

Sequence similaritiesi

Belongs to the thioredoxin family. Plant H-type subfamily.Sequence analysis
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

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]
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.

P85801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLCLAKRNH DADDDEPHIE LAGGNVHLIT TKERWDQKLS EASRDGKIVL
60 70 80 90 100
ANFSARWCGP CKQIAPYYIE LSENYPSLMF LVIDVDELSD FSASWEIKAT
110 120 130
PTFFFLRDGQ QVDKLVGANK PELHKKITAI LDSLPPSDK
Length:139
Mass (Da):15,647
Last modified:June 10, 2008 - v1
Checksum:i19631E2A8A4ADDD4
GO

Mass spectrometryi

Molecular mass is 15515.375±0.3 Da from positions 2 - 139. Determined by ESI. 1 Publication

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3D21X-ray2.15A/B1-139[»]
3D22X-ray1.60A1-139[»]
ProteinModelPortaliP85801.
SMRiP85801.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP85801.

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]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXH_POPJC
AccessioniPrimary (citable) accession number: P85801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: November 2, 2016
This is version 39 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, 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

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 one 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.