Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin M1, chloroplastic

Gene

At1g03680

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

Functioni

Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under reducing conditions, activates the glyceraldehyde-3-phosphate dehydrogenase and the phosphoribulokinase, and inhibits. the glucose-6-phosphate dehydrogenase. Activates NADP-malate dehydrogenase.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei98 – 981Deprotonates C-terminal active site CysBy similarity
Active sitei104 – 1041NucleophileBy similarity
Sitei105 – 1051Contributes to redox potential valueBy similarity
Sitei106 – 1061Contributes to redox potential valueBy similarity
Active sitei107 – 1071NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: GO_Central
  • cellular response to oxidative stress Source: GO_Central
  • glycerol ether metabolic process Source: InterPro
  • negative regulation of catalytic activity Source: UniProtKB
  • oxidation-reduction process Source: GO_Central
  • positive regulation of catalytic activity Source: UniProtKB
  • protein folding Source: GO_Central
  • regulation of carbohydrate metabolic process Source: UniProtKB
  • response to cold Source: TAIR
  • sulfate assimilation Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin M1, chloroplastic
Short name:
AtTrxm1
Gene namesi
Ordered Locus Names:At1g03680
ORF Names:F21B7.28, F21B7_7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G03680.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • chloroplast envelope Source: TAIR
  • chloroplast stroma Source: TAIR
  • stromule Source: TAIR
  • thylakoid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4848ChloroplastSequence analysisAdd
BLAST
Chaini49 – 179131Thioredoxin M1, chloroplasticPRO_0000034162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi104 ↔ 107Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO48737.
PRIDEiO48737.

Expressioni

Gene expression databases

GenevisibleiO48737. AT.

Interactioni

Protein-protein interaction databases

BioGridi24671. 3 interactions.
IntActiO48737. 1 interaction.
STRINGi3702.AT1G03680.1.

Structurei

3D structure databases

ProteinModelPortaliO48737.
SMRiO48737. Positions 79-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 179113ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0910. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiO48737.
KOiK03671.
OMAiSEMRIAS.
PhylomeDBiO48737.

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.
TIGRFAMsiTIGR01068. thioredoxin. 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.

O48737-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAYTCTSRP PISIRSEMRI ASSPTGSFST RQMFSVLPES SGLRTRVSLS
60 70 80 90 100
SLSKNSRVSR LRRGVICEAQ DTATGIPVVN DSTWDSLVLK ADEPVFVDFW
110 120 130 140 150
APWCGPCKMI DPIVNELAQK YAGQFKFYKL NTDESPATPG QYGVRSIPTI
160 170
MIFVNGEKKD TIIGAVSKDT LATSINKFL
Length:179
Mass (Da):19,665
Last modified:June 1, 1998 - v1
Checksum:i35B9E7C1D132F492
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095749 mRNA. Translation: AAF15948.1.
AC002560 Genomic DNA. Translation: AAF86525.1.
CP002684 Genomic DNA. Translation: AEE27596.1.
BT004295 mRNA. Translation: AAO42293.1.
BT005525 mRNA. Translation: AAO63945.1.
PIRiT00893.
RefSeqiNP_849585.1. NM_179254.6.
UniGeneiAt.20253.

Genome annotation databases

EnsemblPlantsiAT1G03680.1; AT1G03680.1; AT1G03680.
GeneIDi839436.
GrameneiAT1G03680.1; AT1G03680.1; AT1G03680.
KEGGiath:AT1G03680.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095749 mRNA. Translation: AAF15948.1.
AC002560 Genomic DNA. Translation: AAF86525.1.
CP002684 Genomic DNA. Translation: AEE27596.1.
BT004295 mRNA. Translation: AAO42293.1.
BT005525 mRNA. Translation: AAO63945.1.
PIRiT00893.
RefSeqiNP_849585.1. NM_179254.6.
UniGeneiAt.20253.

3D structure databases

ProteinModelPortaliO48737.
SMRiO48737. Positions 79-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24671. 3 interactions.
IntActiO48737. 1 interaction.
STRINGi3702.AT1G03680.1.

Proteomic databases

PaxDbiO48737.
PRIDEiO48737.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G03680.1; AT1G03680.1; AT1G03680.
GeneIDi839436.
GrameneiAT1G03680.1; AT1G03680.1; AT1G03680.
KEGGiath:AT1G03680.

Organism-specific databases

TAIRiAT1G03680.

Phylogenomic databases

eggNOGiKOG0910. Eukaryota.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiO48737.
KOiK03671.
OMAiSEMRIAS.
PhylomeDBiO48737.

Enzyme and pathway databases

ReactomeiR-ATH-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiO48737.

Gene expression databases

GenevisibleiO48737. AT.

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.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Arabidopsis thaliana genome encodes at least four thioredoxins m and a new prokaryotic-like thioredoxin."
    Mestres-Ortega D., Meyer Y.
    Gene 240:307-316(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Proteomics of the chloroplast envelope membranes from Arabidopsis thaliana."
    Ferro M., Salvi D., Brugiere S., Miras S., Kowalski S., Louwagie M., Garin J., Joyard J., Rolland N.
    Mol. Cell. Proteomics 2:325-345(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Wassilewskija.
  6. "Redox regulation of chloroplastic glucose-6-phosphate dehydrogenase: a new role for f-type thioredoxin."
    Nee G., Zaffagnini M., Trost P., Issakidis-Bourguet E.
    FEBS Lett. 583:2827-2832(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Prompt and easy activation by specific thioredoxins of calvin cycle enzymes of Arabidopsis thaliana associated in the GAPDH/CP12/PRK supramolecular complex."
    Marri L., Zaffagnini M., Collin V., Issakidis-Bourguet E., Lemaire S.D., Pupillo P., Sparla F., Miginiac-Maslow M., Trost P.
    Mol. Plant 2:259-269(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "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.
  9. Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiTRXM1_ARATH
AccessioniPrimary (citable) accession number: O48737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 1998
Last modified: February 17, 2016
This is version 134 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.