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Bifunctional monothiol glutaredoxin-S16, chloroplastic (AtGrxS16) (Atypical GIY-YIG endonuclease) (EC 3.1.-.-) (CAX-interacting protein 2) (CAXIP1-like protein)

 GRS16_ARATH             Reviewed;         293 AA.
Q8H7F6; O80451; Q8LD13;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-OCT-2017, entry version 98.
RecName: Full=Bifunctional monothiol glutaredoxin-S16, chloroplastic {ECO:0000303|PubMed:15170506};
Short=AtGrxS16 {ECO:0000303|PubMed:15170506};
AltName: Full=Atypical GIY-YIG endonuclease {ECO:0000303|PubMed:23690600};
EC=3.1.-.-;
AltName: Full=CAX-interacting protein 2 {ECO:0000303|PubMed:12480930};
AltName: Full=CAXIP1-like protein {ECO:0000303|PubMed:12480930};
Flags: Precursor;
Name=GRXS16 {ECO:0000303|PubMed:15170506};
Synonyms=CXIP2 {ECO:0000303|PubMed:12480930};
OrderedLocusNames=At2g38270 {ECO:0000312|Araport:AT2G38270};
ORFNames=F16M14.20 {ECO:0000312|EMBL:AAC27175.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12480930; DOI=10.1074/jbc.M210883200;
Cheng N.-H., Hirschi K.D.;
"Cloning and characterization of CXIP1 A novel PICOT domain-containing
Arabidopsis protein that associates with CAX1.";
J. Biol. Chem. 278:6503-6509(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Stracke R., Palme K.;
"Signal peptide selection derived cDNAs from Arabidopsis thaliana
leaves and guard cells.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15170506; DOI=10.1007/s00018-004-3410-y;
Rouhier N., Gelhaye E., Jacquot J.-P.;
"Plant glutaredoxins: still mysterious reducing systems.";
Cell. Mol. Life Sci. 61:1266-1277(2004).
[9]
GENE FAMILY.
PubMed=16720602; DOI=10.1093/jxb/erl001;
Rouhier N., Couturier J., Jacquot J.-P.;
"Genome-wide analysis of plant glutaredoxin systems.";
J. Exp. Bot. 57:1685-1696(2006).
[10]
INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND MUTAGENESIS OF
CYS-219.
PubMed=24203231; DOI=10.1093/mp/sst156;
Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D.,
Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
"Monothiol glutaredoxin-BolA interactions: redox control of
Arabidopsis thaliana BolA2 and SufE1.";
Mol. Plant 7:187-205(2014).
[11]
FUNCTION, AND INTERACTION WITH BOLA1.
PubMed=24714563; DOI=10.4161/psb.28564;
Dhalleine T., Rouhier N., Couturier J.;
"Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
Plant Signal. Behav. 9:E28564-E28564(2014).
[12]
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, AND SUBCELLULAR LOCATION.
PubMed=23690600; DOI=10.1073/pnas.1306899110;
Liu X., Liu S., Feng Y., Liu J.Z., Chen Y., Pham K., Deng H.,
Hirschi K.D., Wang X., Cheng N.;
"Structural insights into the N-terminal GIY-YIG endonuclease activity
of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.";
Proc. Natl. Acad. Sci. U.S.A. 110:9565-9570(2013).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:23690600, ECO:0000269|PubMed:24714563,
ECO:0000305}.
-!- ENZYME REGULATION: The formation of an intramolecular disulfide
bond negatively regulates both the N-terminal endonuclease and the
C-terminal glutaredoxin activities. {ECO:0000269|PubMed:23690600}.
-!- SUBUNIT: [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).
{ECO:0000269|PubMed:23690600, ECO:0000269|PubMed:24203231,
ECO:0000269|PubMed:24714563}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:23690600}.
-!- DOMAIN: The N-terminal domain (NTD) (63-170) has an intrinsic
Mg(2+)-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. {ECO:0000269|PubMed:23690600}.
-!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY157989; AAO19648.1; -; mRNA.
EMBL; AF083698; AAN60257.1; -; mRNA.
EMBL; AC003028; AAC27175.1; -; Genomic_DNA.
EMBL; CP002685; AEC09515.1; -; Genomic_DNA.
EMBL; AK117441; BAC42106.1; -; mRNA.
EMBL; BT004974; AAO50507.1; -; mRNA.
EMBL; AY086273; AAM64346.1; -; mRNA.
PIR; T01258; T01258.
RefSeq; NP_565885.1; NM_129383.3.
UniGene; At.25559; -.
UniGene; At.71438; -.
PDB; 2LWF; NMR; -; A=63-170.
PDBsum; 2LWF; -.
ProteinModelPortal; Q8H7F6; -.
SMR; Q8H7F6; -.
BioGrid; 3749; 12.
IntAct; Q8H7F6; 7.
STRING; 3702.AT2G38270.1; -.
PaxDb; Q8H7F6; -.
PRIDE; Q8H7F6; -.
EnsemblPlants; AT2G38270.1; AT2G38270.1; AT2G38270.
GeneID; 818407; -.
Gramene; AT2G38270.1; AT2G38270.1; AT2G38270.
KEGG; ath:AT2G38270; -.
Araport; AT2G38270; -.
TAIR; locus:2042887; AT2G38270.
eggNOG; KOG0911; Eukaryota.
eggNOG; COG0278; LUCA.
HOGENOM; HOG000243994; -.
InParanoid; Q8H7F6; -.
OMA; SWKSWME; -.
OrthoDB; EOG09360HE3; -.
PhylomeDB; Q8H7F6; -.
PRO; PR:Q8H7F6; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q8H7F6; baseline and differential.
Genevisible; Q8H7F6; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0006812; P:cation transport; IDA:TAIR.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
CDD; cd03028; GRX_PICOT_like; 1.
Gene3D; 3.40.1440.10; -; 1.
InterPro; IPR035901; GIY-YIG_endonuc_sf.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR033658; GRX_PICOT-like.
InterPro; IPR004480; Monothiol_GRX-rel.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10293; PTHR10293; 1.
Pfam; PF00462; Glutaredoxin; 1.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR00365; TIGR00365; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Chloroplast; Complete proteome; Disulfide bond;
Hydrolase; Iron; Iron-sulfur; Metal-binding; Multifunctional enzyme;
Plastid; Redox-active center; Reference proteome; Transit peptide.
TRANSIT 1 62 Chloroplast. {ECO:0000255}.
CHAIN 63 293 Bifunctional monothiol glutaredoxin-S16,
chloroplastic.
/FTId=PRO_0000268736.
DOMAIN 194 293 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
REGION 276 277 Glutathione binding.
{ECO:0000250|UniProtKB:P0AC69}.
METAL 219 219 Iron-sulfur (2Fe-2S); shared with dimeric
partner. {ECO:0000250|UniProtKB:P0AC69}.
BINDING 211 211 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 251 251 Glutathione.
{ECO:0000250|UniProtKB:P0AC69}.
BINDING 263 263 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P0AC69}.
DISULFID 123 219 {ECO:0000269|PubMed:23690600}.
MUTAGEN 90 90 Y->F: Strongly reduced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 101 101 F->Y: Enhanced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 111 111 S->A: Strongly reduced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 111 111 S->R: Slightly reduced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 115 115 H->F: Strongly reduced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 123 123 C->S: Increased glutaredoxin activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 143 143 W->A,E: Slightly reduced nuclease
activity. {ECO:0000269|PubMed:23690600}.
MUTAGEN 161 161 N->L: Slightly reduced nuclease activity.
{ECO:0000269|PubMed:23690600}.
MUTAGEN 219 219 C->S: Decreased interactions with BOLA
proteins and loss of interaction with
SUFE1. {ECO:0000269|PubMed:24203231}.
CONFLICT 194 194 E -> G (in Ref. 2; AAN60257).
{ECO:0000305}.
HELIX 69 71 {ECO:0000244|PDB:2LWF}.
STRAND 73 77 {ECO:0000244|PDB:2LWF}.
HELIX 80 82 {ECO:0000244|PDB:2LWF}.
STRAND 86 93 {ECO:0000244|PDB:2LWF}.
STRAND 99 106 {ECO:0000244|PDB:2LWF}.
HELIX 108 118 {ECO:0000244|PDB:2LWF}.
HELIX 120 122 {ECO:0000244|PDB:2LWF}.
STRAND 124 130 {ECO:0000244|PDB:2LWF}.
HELIX 136 153 {ECO:0000244|PDB:2LWF}.
TURN 159 163 {ECO:0000244|PDB:2LWF}.
TURN 167 169 {ECO:0000244|PDB:2LWF}.
SEQUENCE 293 AA; 32206 MW; 6B2E6337F8C5F050 CRC64;
MAAITISSSL HASASPRVVR PHVSRNTPVI TLYSRFTPSF SFPSLSFTLR DTAPSRRRSF
FIASAVKSLT ETELLPITEA DSIPSASGVY AVYDKSDELQ FVGISRNIAA SVSAHLKSVP
ELCGSVKVGI VEEPDKAVLT QAWKLWIEEH IKVTGKVPPG NKSGNNTFVK QTPRKKSDIR
LTPGRHVELT VPLEELIDRL VKESKVVAFI KGSRSAPQCG FSQRVVGILE SQGVDYETVD
VLDDEYNHGL RETLKNYSNW PTFPQIFVKG ELVGGCDILT SMYENGELAN ILN


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