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Glutaredoxin-C5, chloroplastic (AtGrxC5)

 GRXC5_ARATH             Reviewed;         174 AA.
Q8GWS0; Q9SVU1;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 101.
RecName: Full=Glutaredoxin-C5, chloroplastic {ECO:0000303|PubMed:15170506};
Short=AtGrxC5 {ECO:0000303|PubMed:15170506};
Flags: Precursor;
Name=GRXC5 {ECO:0000303|PubMed:15170506};
OrderedLocusNames=At4g28730 {ECO:0000312|Araport:AT4G28730};
ORFNames=F16A16.160 {ECO:0000312|EMBL:CAA22979.1};
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
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).
[4]
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).
[5]
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).
[6]
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).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-52, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER MET-51, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[8]
LACK OF INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4.
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 64-174 OF APO- AND HOLOFORMS
IN COMPLEX WITH GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
SUBCELLULAR LOCATION, INDUCTION BY COLD, SUBUNIT, MUTAGENESIS OF
CYS-90; CYS-93; CYS-141 AND CYS-148, AND GLUTATHIONYLATION AT CYS-90
AND CYS-148.
PubMed=21632542; DOI=10.1074/jbc.M111.228726;
Couturier J., Stroher E., Albetel A.N., Roret T., Muthuramalingam M.,
Tarrago L., Seidel T., Tsan P., Jacquot J.P., Johnson M.K.,
Dietz K.J., Didierjean C., Rouhier N.;
"Arabidopsis chloroplastic glutaredoxin C5 as a model to explore
molecular determinants for iron-sulfur cluster binding into
glutaredoxins.";
J. Biol. Chem. 286:27515-27527(2011).
-!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
the presence of NADPH and glutathione reductase. Reduces low
molecular weight disulfides and proteins. Can assemble a [2Fe-2S]
cluster, but cannot transfer it to an apoferredoxin.
{ECO:0000269|PubMed:21632542}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.20 mM for glutathionylated beta-mercaptoethanol
{ECO:0000269|PubMed:21632542};
KM=0.21 mM for dehydroascorbate {ECO:0000269|PubMed:21632542};
KM=3.6 mM for reduced glutathione {ECO:0000269|PubMed:21632542};
Note=kcat is 1.21 sec(-1) with glutathionylated beta-
mercaptoethanol as substrate. kcat is 0.23 sec(-1) with
dehydroascorbate as substrate. kcat is 0.69 sec(-1) with reduced
glutathione as substrate. {ECO:0000269|PubMed:21632542};
-!- SUBUNIT: Monomeric apoprotein and homodimeric holoprotein
containing a [2Fe-2S] cluster (PubMed:21632542). No in vitro
interactions with SUFE1, BOLA1, BOLA2 or BOLA4 (PubMed:24203231).
{ECO:0000269|PubMed:21632542, ECO:0000269|PubMed:24203231}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:21632542}.
-!- INDUCTION: Up-regulated by cold treatment.
{ECO:0000269|PubMed:21632542}.
-!- PTM: Glutathionylated. {ECO:0000269|PubMed:21632542}.
-!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA22979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB81461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL035353; CAA22979.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161573; CAB81461.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE85535.1; -; Genomic_DNA.
EMBL; AK118672; BAC43267.1; -; mRNA.
EMBL; BT003703; AAO39931.1; -; mRNA.
PIR; T04526; T04526.
RefSeq; NP_194602.2; NM_119017.5.
UniGene; At.31993; -.
PDB; 3RHB; X-ray; 1.20 A; A=64-174.
PDB; 3RHC; X-ray; 2.40 A; A/B=64-174.
PDBsum; 3RHB; -.
PDBsum; 3RHC; -.
ProteinModelPortal; Q8GWS0; -.
SMR; Q8GWS0; -.
BioGrid; 14281; 5.
IntAct; Q8GWS0; 2.
STRING; 3702.AT4G28730.1; -.
PaxDb; Q8GWS0; -.
PRIDE; Q8GWS0; -.
EnsemblPlants; AT4G28730.1; AT4G28730.1; AT4G28730.
GeneID; 828994; -.
Gramene; AT4G28730.1; AT4G28730.1; AT4G28730.
KEGG; ath:AT4G28730; -.
Araport; AT4G28730; -.
TAIR; locus:2117793; AT4G28730.
eggNOG; KOG1752; Eukaryota.
eggNOG; COG0695; LUCA.
HOGENOM; HOG000095204; -.
InParanoid; Q8GWS0; -.
OMA; ARMEDSV; -.
OrthoDB; EOG09360R46; -.
PhylomeDB; Q8GWS0; -.
EvolutionaryTrace; Q8GWS0; -.
PRO; PR:Q8GWS0; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q8GWS0; baseline and differential.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0004362; F:glutathione-disulfide reductase activity; IDA:TAIR.
GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
InterPro; IPR002109; Glutaredoxin.
InterPro; IPR011899; Glutaredoxin_euk/vir.
InterPro; IPR014025; Glutaredoxin_subgr.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00462; Glutaredoxin; 1.
PRINTS; PR00160; GLUTAREDOXIN.
SUPFAM; SSF52833; SSF52833; 1.
TIGRFAMs; TIGR02180; GRX_euk; 1.
PROSITE; PS51354; GLUTAREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chloroplast; Complete proteome;
Disulfide bond; Electron transport; Glutathionylation; Plastid;
Redox-active center; Reference proteome; Transit peptide; Transport.
TRANSIT 1 51 Chloroplast.
{ECO:0000244|PubMed:22223895,
ECO:0000305}.
CHAIN 52 174 Glutaredoxin-C5, chloroplastic.
/FTId=PRO_0000268712.
DOMAIN 93 171 Glutaredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00686}.
BINDING 135 135 Glutathione; via amide nitrogen and
carbonyl oxygen.
{ECO:0000269|PubMed:21632542}.
BINDING 148 148 Glutathione; via amide nitrogen.
{ECO:0000269|PubMed:21632542}.
BINDING 149 149 Glutathione; via amide nitrogen.
{ECO:0000269|PubMed:21632542}.
MOD_RES 52 52 N-acetylthreonine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 90 90 S-glutathionyl cysteine; partial.
{ECO:0000269|PubMed:21632542}.
MOD_RES 148 148 S-glutathionyl cysteine; partial.
{ECO:0000269|PubMed:21632542}.
DISULFID 90 93 Redox-active.
{ECO:0000250|UniProtKB:P25373}.
MUTAGEN 90 90 C->S: Loss of Fe-S cluster incorporation
and loss of glutaredoxin activity.
{ECO:0000269|PubMed:21632542}.
MUTAGEN 93 93 C->S: Loss of Fe-S cluster incorporation,
but increased glutaredoxin activity.
{ECO:0000269|PubMed:21632542}.
MUTAGEN 141 141 C->S: No effect on Fe-S cluster
incorporation or on glutaredoxin
activity. {ECO:0000269|PubMed:21632542}.
MUTAGEN 148 148 C->S: No effect on Fe-S cluster
incorporation or on glutaredoxin
activity. {ECO:0000269|PubMed:21632542}.
HELIX 68 79 {ECO:0000244|PDB:3RHB}.
STRAND 80 86 {ECO:0000244|PDB:3RHB}.
HELIX 91 102 {ECO:0000244|PDB:3RHB}.
STRAND 108 111 {ECO:0000244|PDB:3RHB}.
HELIX 112 114 {ECO:0000244|PDB:3RHB}.
HELIX 118 130 {ECO:0000244|PDB:3RHB}.
STRAND 137 140 {ECO:0000244|PDB:3RHB}.
STRAND 143 147 {ECO:0000244|PDB:3RHB}.
HELIX 148 156 {ECO:0000244|PDB:3RHB}.
HELIX 159 164 {ECO:0000244|PDB:3RHB}.
SEQUENCE 174 AA; 18814 MW; D7912FC4FBB01743 CRC64;
MAVTAFNTLK LVSSSLDPIP SVSCSSYSFS LIYVGSPYKR CLKQSCSVRA MTSSSSAASS
SSSSFGSRME ESIRKTVTEN TVVIYSKTWC SYCTEVKTLF KRLGVQPLVV ELDQLGPQGP
QLQKVLERLT GQHTVPNVFV CGKHIGGCTD TVKLNRKGDL ELMLAEANGK NGQS


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