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Protein

Bifunctional monothiol glutaredoxin-S16, chloroplastic

Gene

GRXS16

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

Functioni

May only reduce GSH-thiol disulfides, but not protein disulfides (Probable). Participates probably to the maturation of iron-sulfur proteins and to the regulation of the redox state of the BOLA proteins (Probable). The GRXS16-BOLA1 heterodimer binds a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563). Able to cleave linearized DNA in vitro (PubMed:23690600).Curated2 Publications

Enzyme regulationi

The formation of an intramolecular disulfide bond negatively regulates both the N-terminal endonuclease and the C-terminal glutaredoxin activities.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei211 – 2111GlutathioneBy similarity
Metal bindingi219 – 2191Iron-sulfur (2Fe-2S); shared with dimeric partnerBy similarity
Binding sitei251 – 2511GlutathioneBy similarity
Binding sitei263 – 2631Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cation transport Source: TAIR
  2. cell redox homeostasis Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional monothiol glutaredoxin-S16, chloroplastic1 Publication
Short name:
AtGrxS161 Publication
Alternative name(s):
Atypical GIY-YIG endonuclease1 Publication (EC:3.1.-.-)
CAX-interacting protein 21 Publication
CAXIP1-like protein1 Publication
Gene namesi
Name:GRXS161 Publication
Synonyms:CXIP21 Publication
Ordered Locus Names:At2g38270Imported
ORF Names:F16M14.20Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G38270.

Subcellular locationi

Plastidchloroplast 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901Y → F: Strongly reduced nuclease activity. 1 Publication
Mutagenesisi101 – 1011F → Y: Enhanced nuclease activity. 1 Publication
Mutagenesisi111 – 1111S → A: Strongly reduced nuclease activity. 1 Publication
Mutagenesisi111 – 1111S → R: Slightly reduced nuclease activity. 1 Publication
Mutagenesisi115 – 1151H → F: Strongly reduced nuclease activity. 1 Publication
Mutagenesisi123 – 1231C → S: Increased glutaredoxin activity. 1 Publication
Mutagenesisi143 – 1431W → A or E: Slightly reduced nuclease activity. 1 Publication
Mutagenesisi161 – 1611N → L: Slightly reduced nuclease activity. 1 Publication
Mutagenesisi219 – 2191C → S: Decreased interactions with BOLA proteins and loss of interaction with SUFE1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6262ChloroplastSequence AnalysisAdd
BLAST
Chaini63 – 293231Bifunctional monothiol glutaredoxin-S16, chloroplasticPRO_0000268736Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi123 ↔ 2191 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8H7F6.
PRIDEiQ8H7F6.

Expressioni

Gene expression databases

GenevestigatoriQ8H7F6.

Interactioni

Subunit structurei

[2Fe-2S]-bridged holo-homodimer (PubMed:23690600). Interacts in vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231). Interacts in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231, PubMed:24714563).3 Publications

Protein-protein interaction databases

BioGridi3749. 12 interactions.
IntActiQ8H7F6. 7 interactions.
STRINGi3702.AT2G38270.1-P.

Structurei

Secondary structure

1
293
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 713Combined sources
Beta strandi73 – 775Combined sources
Helixi80 – 823Combined sources
Beta strandi86 – 938Combined sources
Beta strandi99 – 1068Combined sources
Helixi108 – 11811Combined sources
Helixi120 – 1223Combined sources
Beta strandi124 – 1307Combined sources
Helixi136 – 15318Combined sources
Turni159 – 1635Combined sources
Turni167 – 1693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWFNMR-A63-170[»]
ProteinModelPortaliQ8H7F6.
SMRiQ8H7F6. Positions 62-172, 195-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 293100GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni276 – 2772Glutathione bindingBy similarity

Domaini

The N-terminal domain (NTD) (63-170) has an intrinsic Mg2+-dependent endonuclease activity in vitro (PubMed:23690600). The glutaredoxin (GRX) domain (194-293) alone is able to complement yeast grx5 cells in vitro, but not the full length GRXS16 protein.1 Publication

Sequence similaritiesi

Belongs to the glutaredoxin family. CGFS subfamily.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiCOG0278.
HOGENOMiHOG000243994.
InParanoidiQ8H7F6.
OMAiILTSMHE.
PhylomeDBiQ8H7F6.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8H7F6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAITISSSL HASASPRVVR PHVSRNTPVI TLYSRFTPSF SFPSLSFTLR
60 70 80 90 100
DTAPSRRRSF FIASAVKSLT ETELLPITEA DSIPSASGVY AVYDKSDELQ
110 120 130 140 150
FVGISRNIAA SVSAHLKSVP ELCGSVKVGI VEEPDKAVLT QAWKLWIEEH
160 170 180 190 200
IKVTGKVPPG NKSGNNTFVK QTPRKKSDIR LTPGRHVELT VPLEELIDRL
210 220 230 240 250
VKESKVVAFI KGSRSAPQCG FSQRVVGILE SQGVDYETVD VLDDEYNHGL
260 270 280 290
RETLKNYSNW PTFPQIFVKG ELVGGCDILT SMYENGELAN ILN
Length:293
Mass (Da):32,206
Last modified:December 12, 2006 - v2
Checksum:i6B2E6337F8C5F050
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941E → G in AAN60257 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157989 mRNA. Translation: AAO19648.1.
AF083698 mRNA. Translation: AAN60257.1.
AC003028 Genomic DNA. Translation: AAC27175.1.
CP002685 Genomic DNA. Translation: AEC09515.1.
AK117441 mRNA. Translation: BAC42106.1.
BT004974 mRNA. Translation: AAO50507.1.
AY086273 mRNA. Translation: AAM64346.1.
PIRiT01258.
RefSeqiNP_565885.1. NM_129383.2.
UniGeneiAt.25559.
At.71438.

Genome annotation databases

EnsemblPlantsiAT2G38270.1; AT2G38270.1; AT2G38270.
GeneIDi818407.
KEGGiath:AT2G38270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY157989 mRNA. Translation: AAO19648.1.
AF083698 mRNA. Translation: AAN60257.1.
AC003028 Genomic DNA. Translation: AAC27175.1.
CP002685 Genomic DNA. Translation: AEC09515.1.
AK117441 mRNA. Translation: BAC42106.1.
BT004974 mRNA. Translation: AAO50507.1.
AY086273 mRNA. Translation: AAM64346.1.
PIRiT01258.
RefSeqiNP_565885.1. NM_129383.2.
UniGeneiAt.25559.
At.71438.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWFNMR-A63-170[»]
ProteinModelPortaliQ8H7F6.
SMRiQ8H7F6. Positions 62-172, 195-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3749. 12 interactions.
IntActiQ8H7F6. 7 interactions.
STRINGi3702.AT2G38270.1-P.

Proteomic databases

PaxDbiQ8H7F6.
PRIDEiQ8H7F6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G38270.1; AT2G38270.1; AT2G38270.
GeneIDi818407.
KEGGiath:AT2G38270.

Organism-specific databases

TAIRiAT2G38270.

Phylogenomic databases

eggNOGiCOG0278.
HOGENOMiHOG000243994.
InParanoidiQ8H7F6.
OMAiILTSMHE.
PhylomeDBiQ8H7F6.

Gene expression databases

GenevestigatoriQ8H7F6.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR004480. Monothiol_GRX-rel.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR10293. PTHR10293. 1 hit.
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR00365. TIGR00365. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of CXIP1 A novel PICOT domain-containing Arabidopsis protein that associates with CAX1."
    Cheng N.-H., Hirschi K.D.
    J. Biol. Chem. 278:6503-6509(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells."
    Stracke R., Palme K.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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.
  7. "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].
  8. "Plant glutaredoxins: still mysterious reducing systems."
    Rouhier N., Gelhaye E., Jacquot J.-P.
    Cell. Mol. Life Sci. 61:1266-1277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  9. "Genome-wide analysis of plant glutaredoxin systems."
    Rouhier N., Couturier J., Jacquot J.-P.
    J. Exp. Bot. 57:1685-1696(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  10. "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1."
    Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.
    Mol. Plant 7:187-205(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, MUTAGENESIS OF CYS-219.
  11. "Putative roles of glutaredoxin-BolA holo-heterodimers in plants."
    Dhalleine T., Rouhier N., Couturier J.
    Plant Signal. Behav. 9:E28564-E28564(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BOLA1.
  12. "Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts."
    Liu X., Liu S., Feng Y., Liu J.Z., Chen Y., Pham K., Deng H., Hirschi K.D., Wang X., Cheng N.
    Proc. Natl. Acad. Sci. U.S.A. 110:9565-9570(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 63-170, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-90; PHE-101; SER-111; HIS-115; CYS-123; TRP-143 AND ASN-161, SUBUNIT, DISULFIDE BOND, ENZYME REGULATION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiGRS16_ARATH
AccessioniPrimary (citable) accession number: Q8H7F6
Secondary accession number(s): O80451, Q8LD13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: March 4, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, 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.