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Reviewed, UniProtKB/Swiss-Prot P23400 (TRXM_CHLRE)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Thioredoxin M-type, chloroplastic
      Short name=Trx-M
Alternative name(s):
    Thioredoxin-CH2
Gene names
Name: TRXM
OrganismChlamydomonas reinhardtii
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

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Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase By similarity.

Subcellular location

Plastid › chloroplast By similarity.

Sequence similarities

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

Contains 1 thioredoxin domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Chloroplast Ref.3
Chain35 – 140106Thioredoxin M-type, chloroplastic
PRO_0000034174

Regions

Domain35 – 140106Thioredoxin

Sites

Active site641Nucleophile
Active site671Nucleophile
Site581Deprotonates C-terminal active site Cys
Site651Contributes to redox potential value
Site661Contributes to redox potential value

Amino acid modifications

Disulfide bond64 ↔ 67Redox-active Ref.3

Experimental info

Sequence conflict41 – 422DD → EE AA sequence Ref.3
Sequence conflict871C → E AA sequence Ref.3
Sequence conflict1191C → D AA sequence Ref.3

Secondary structure

1 .................... 140
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P23400-1 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: B9CB842F91D872CA

FASTA14015,102
        10         20         30         40         50         60 
MALVARRAAV PSARSSARPA FARAAPRRSV VVRAEAGAVN DDTFKNVVLE SSVPVLVDFW 

        70         80         90        100        110        120 
APWCGPCRII APVVDEIAGE YKDKLKCVKL NTDESPNVAS EYGIRSIPTI MVFKGGKKCE 

       130        140 
TIIGAVPKAT IVQTVEKYLN

« Hide

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References

[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: 7632918] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"PCR cloning of a nucleotidic sequence coding for the mature part of Chlamydomonas reinhardtii thioredoxin Ch2."
Jacquot J.-P., Stein M., Hodges M., Miginiac-Maslow M.
Nucleic Acids Res. 20:617-617(1992) [PubMed: 1741302] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-140.
[3]"Purification, characterization, and complete amino acid sequence of a thioredoxin from a green alga, Chlamydomonas reinhardtii."
Decottignies P., Schmitter J.-M., Jacquot J.-P., Dutka S., Picaud A., Gadal P.
Arch. Biochem. Biophys. 280:112-121(1990) [PubMed: 2191628] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-140, DISULFIDE BOND.
Strain: 137c / CC-125.
[4]"NMR structure and dynamic of the chloroplast thioredoxin M CH2 from the green alga Chlamydomonas reinhardtii."
Lancelin J.-M., Guilhaudis L., Krimm I., Blackledge M.J., Marion D., Jacquot J.-P.
Submitted (NOV-1999) to the PDB data bank
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X80888 Genomic DNA. Translation: CAA56851.1.
X78821 mRNA. Translation: CAA55398.1.
X62335 mRNA. Translation: CAA44209.1.
PIRS57774.
RefSeqXP_001690314.1.
UniGeneCre.5609

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DBYNMR-A35-140[»]
ModBaseSearch...

Proteomic databases

PRIDEP23400.

Genome annotation databases

GeneID5715906.
KEGGcre:CHLREDRAFT_136413.

Family and domain databases

InterProIPR005746. Thioredoxin.
IPR017936. Thioredoxin-like.
IPR006662. Thioredoxin-like_subdom.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHERPTHR10438. Trx. 1 hit.
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
PRINTSPR00421. THIOREDOXIN.
TIGRFAMsTIGR01068. thioredoxin. 1 hit.
PROSITEPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameTRXM_CHLRE
AccessionPrimary (citable) accession number: P23400
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: October 1, 1996
Last modified: June 16, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents