ID   GRS16_ARATH             Reviewed;         293 AA.
AC   Q8H7F6; O80451; Q8LD13;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Bifunctional monothiol glutaredoxin-S16, chloroplastic {ECO:0000303|PubMed:15170506};
DE            Short=AtGrxS16 {ECO:0000303|PubMed:15170506};
DE   AltName: Full=Atypical GIY-YIG endonuclease {ECO:0000303|PubMed:23690600};
DE            EC=3.1.-.-;
DE   AltName: Full=CAX-interacting protein 2 {ECO:0000303|PubMed:12480930};
DE   AltName: Full=CAXIP1-like protein {ECO:0000303|PubMed:12480930};
DE   Flags: Precursor;
GN   Name=GRXS16 {ECO:0000303|PubMed:15170506};
GN   Synonyms=CXIP2 {ECO:0000303|PubMed:12480930};
GN   OrderedLocusNames=At2g38270 {ECO:0000312|Araport:AT2G38270};
GN   ORFNames=F16M14.20 {ECO:0000312|EMBL:AAC27175.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12480930; DOI=10.1074/jbc.m210883200;
RA   Cheng N.-H., Hirschi K.D.;
RT   "Cloning and characterization of CXIP1 A novel PICOT domain-containing
RT   Arabidopsis protein that associates with CAX1.";
RL   J. Biol. Chem. 278:6503-6509(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Stracke R., Palme K.;
RT   "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT   and guard cells.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15170506; DOI=10.1007/s00018-004-3410-y;
RA   Rouhier N., Gelhaye E., Jacquot J.-P.;
RT   "Plant glutaredoxins: still mysterious reducing systems.";
RL   Cell. Mol. Life Sci. 61:1266-1277(2004).
RN   [9]
RP   GENE FAMILY.
RX   PubMed=16720602; DOI=10.1093/jxb/erl001;
RA   Rouhier N., Couturier J., Jacquot J.-P.;
RT   "Genome-wide analysis of plant glutaredoxin systems.";
RL   J. Exp. Bot. 57:1685-1696(2006).
RN   [10]
RP   INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4, AND MUTAGENESIS OF CYS-219.
RX   PubMed=24203231; DOI=10.1093/mp/sst156;
RA   Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M.,
RA   Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
RT   "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis
RT   thaliana BolA2 and SufE1.";
RL   Mol. Plant 7:187-205(2014).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH BOLA1.
RX   PubMed=24714563; DOI=10.4161/psb.28564;
RA   Dhalleine T., Rouhier N., Couturier J.;
RT   "Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
RL   Plant Signal. Behav. 9:E28564-E28564(2014).
RN   [12]
RP   INTERACTION WITH SBP1.
RX   PubMed=30824043; DOI=10.1016/j.plantsci.2019.01.021;
RA   Valassakis C., Dervisi I., Agalou A., Papandreou N., Kapetsis G., Podia V.,
RA   Haralampidis K., Iconomidou V.A., Spaink H.P., Roussis A.;
RT   "Novel interactions of selenium binding protein family with the PICOT
RT   containing proteins AtGRXS14 and AtGRXS16 in Arabidopsis thaliana.";
RL   Plant Sci. 281:102-112(2019).
RN   [13]
RP   STRUCTURE BY NMR OF 63-170, FUNCTION, DOMAIN, MUTAGENESIS OF TYR-90;
RP   PHE-101; SER-111; HIS-115; CYS-123; TRP-143 AND ASN-161, SUBUNIT, DISULFIDE
RP   BOND, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=23690600; DOI=10.1073/pnas.1306899110;
RA   Liu X., Liu S., Feng Y., Liu J.Z., Chen Y., Pham K., Deng H., Hirschi K.D.,
RA   Wang X., Cheng N.;
RT   "Structural insights into the N-terminal GIY-YIG endonuclease activity of
RT   Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:9565-9570(2013).
CC   -!- FUNCTION: May only reduce GSH-thiol disulfides, but not protein
CC       disulfides (Probable). Participates probably to the maturation of iron-
CC       sulfur proteins and to the regulation of the redox state of the BOLA
CC       proteins (Probable). The GRXS16-BOLA1 heterodimer binds a labile,
CC       oxygen sensitive iron-sulfur cluster (PubMed:24714563). Able to cleave
CC       linearized DNA in vitro (PubMed:23690600).
CC       {ECO:0000269|PubMed:23690600, ECO:0000269|PubMed:24714563,
CC       ECO:0000305}.
CC   -!- ACTIVITY REGULATION: The formation of an intramolecular disulfide bond
CC       negatively regulates both the N-terminal endonuclease and the C-
CC       terminal glutaredoxin activities. {ECO:0000269|PubMed:23690600}.
CC   -!- SUBUNIT: [2Fe-2S]-bridged holo-homodimer (PubMed:23690600). Interacts
CC       in vitro with SUFE1, BOLA1, BOLA2 and BOLA4 (PubMed:24203231).
CC       Interacts in vivo only with SUFE1, BOLA1 and BOLA4 (PubMed:24203231,
CC       PubMed:24714563, PubMed:23690600). Interacts with SBP1
CC       (PubMed:30824043). {ECO:0000269|PubMed:23690600,
CC       ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563,
CC       ECO:0000269|PubMed:30824043}.
CC   -!- INTERACTION:
CC       Q8H7F6; Q9XFM0: IAA28; NbExp=3; IntAct=EBI-4424482, EBI-3133404;
CC       Q8H7F6; O81313: IND; NbExp=4; IntAct=EBI-4424482, EBI-4446992;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:23690600}.
CC   -!- DOMAIN: The N-terminal domain (NTD) (63-170) has an intrinsic Mg(2+)-
CC       dependent endonuclease activity in vitro (PubMed:23690600). The
CC       glutaredoxin (GRX) domain (194-293) alone is able to complement yeast
CC       grx5 cells in vitro, but not the full-length GRXS16 protein.
CC       {ECO:0000269|PubMed:23690600}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. CGFS subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AY157989; AAO19648.1; -; mRNA.
DR   EMBL; AF083698; AAN60257.1; -; mRNA.
DR   EMBL; AC003028; AAC27175.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09515.1; -; Genomic_DNA.
DR   EMBL; AK117441; BAC42106.1; -; mRNA.
DR   EMBL; BT004974; AAO50507.1; -; mRNA.
DR   EMBL; AY086273; AAM64346.1; -; mRNA.
DR   PIR; T01258; T01258.
DR   RefSeq; NP_565885.1; NM_129383.3.
DR   PDB; 2LWF; NMR; -; A=63-170.
DR   PDBsum; 2LWF; -.
DR   AlphaFoldDB; Q8H7F6; -.
DR   BMRB; Q8H7F6; -.
DR   SMR; Q8H7F6; -.
DR   BioGRID; 3749; 14.
DR   IntAct; Q8H7F6; 8.
DR   STRING; 3702.Q8H7F6; -.
DR   PaxDb; 3702-AT2G38270-1; -.
DR   ProteomicsDB; 222250; -.
DR   EnsemblPlants; AT2G38270.1; AT2G38270.1; AT2G38270.
DR   GeneID; 818407; -.
DR   Gramene; AT2G38270.1; AT2G38270.1; AT2G38270.
DR   KEGG; ath:AT2G38270; -.
DR   Araport; AT2G38270; -.
DR   TAIR; AT2G38270; CXIP2.
DR   eggNOG; KOG0911; Eukaryota.
DR   HOGENOM; CLU_070932_0_0_1; -.
DR   InParanoid; Q8H7F6; -.
DR   OMA; HMQLTVP; -.
DR   OrthoDB; 1219837at2759; -.
DR   PhylomeDB; Q8H7F6; -.
DR   PRO; PR:Q8H7F6; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q8H7F6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006812; P:monoatomic cation transport; IDA:TAIR.
DR   CDD; cd10457; GIY-YIG_AtGrxS16; 1.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR049620; GIY-YIG_AtGrxS16.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR   PANTHER; PTHR10293:SF45; BIFUNCTIONAL MONOTHIOL GLUTAREDOXIN-S16, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   Genevisible; Q8H7F6; AT.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Chloroplast; Disulfide bond; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Multifunctional enzyme; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide.
FT   TRANSIT         1..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..293
FT                   /note="Bifunctional monothiol glutaredoxin-S16,
FT                   chloroplastic"
FT                   /id="PRO_0000268736"
FT   DOMAIN          194..293
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   BINDING         211
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC69"
FT   BINDING         219
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC69"
FT   BINDING         251
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC69"
FT   BINDING         263
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC69"
FT   BINDING         276..277
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P0AC69"
FT   DISULFID        123..219
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         90
FT                   /note="Y->F: Strongly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         101
FT                   /note="F->Y: Enhanced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         111
FT                   /note="S->A: Strongly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         111
FT                   /note="S->R: Slightly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         115
FT                   /note="H->F: Strongly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         123
FT                   /note="C->S: Increased glutaredoxin activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         143
FT                   /note="W->A,E: Slightly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         161
FT                   /note="N->L: Slightly reduced nuclease activity."
FT                   /evidence="ECO:0000269|PubMed:23690600"
FT   MUTAGEN         219
FT                   /note="C->S: Decreased interactions with BOLA proteins and
FT                   loss of interaction with SUFE1."
FT                   /evidence="ECO:0000269|PubMed:24203231"
FT   CONFLICT        194
FT                   /note="E -> G (in Ref. 2; AAN60257)"
FT                   /evidence="ECO:0000305"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   STRAND          86..93
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   STRAND          99..106
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   HELIX           108..118
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   STRAND          124..130
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   HELIX           136..153
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   TURN            159..163
FT                   /evidence="ECO:0007829|PDB:2LWF"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:2LWF"
SQ   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
//