GRXC5_ARATH
ID GRXC5_ARATH Reviewed; 174 AA.
AC Q8GWS0; Q9SVU1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutaredoxin-C5, chloroplastic {ECO:0000303|PubMed:15170506};
DE Short=AtGrxC5 {ECO:0000303|PubMed:15170506};
DE Flags: Precursor;
GN Name=GRXC5 {ECO:0000303|PubMed:15170506};
GN OrderedLocusNames=At4g28730 {ECO:0000312|Araport:AT4G28730};
GN ORFNames=F16A16.160 {ECO:0000312|EMBL:CAA22979.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER MET-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP LACK OF INTERACTION WITH SUFE1; BOLA1; BOLA2 AND BOLA4.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 64-174 OF APO- AND HOLOFORMS IN
RP COMPLEX WITH GLUTATHIONE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, INDUCTION BY COLD, SUBUNIT, MUTAGENESIS OF CYS-90;
RP CYS-93; CYS-141 AND CYS-148, AND GLUTATHIONYLATION AT CYS-90 AND CYS-148.
RX PubMed=21632542; DOI=10.1074/jbc.m111.228726;
RA Couturier J., Stroher E., Albetel A.N., Roret T., Muthuramalingam M.,
RA Tarrago L., Seidel T., Tsan P., Jacquot J.P., Johnson M.K., Dietz K.J.,
RA Didierjean C., Rouhier N.;
RT "Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular
RT determinants for iron-sulfur cluster binding into glutaredoxins.";
RL J. Biol. Chem. 286:27515-27527(2011).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but
CC cannot transfer it to an apoferredoxin. {ECO:0000269|PubMed:21632542}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for glutathionylated beta-mercaptoethanol
CC {ECO:0000269|PubMed:21632542};
CC KM=0.21 mM for dehydroascorbate {ECO:0000269|PubMed:21632542};
CC KM=3.6 mM for reduced glutathione {ECO:0000269|PubMed:21632542};
CC Note=kcat is 1.21 sec(-1) with glutathionylated beta-mercaptoethanol
CC as substrate. kcat is 0.23 sec(-1) with dehydroascorbate as
CC substrate. kcat is 0.69 sec(-1) with reduced glutathione as
CC substrate. {ECO:0000269|PubMed:21632542};
CC -!- SUBUNIT: Monomeric apoprotein and homodimeric holoprotein containing a
CC [2Fe-2S] cluster (PubMed:21632542). No in vitro interactions with
CC SUFE1, BOLA1, BOLA2 or BOLA4 (PubMed:24203231).
CC {ECO:0000269|PubMed:21632542, ECO:0000269|PubMed:24203231}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21632542}.
CC -!- INDUCTION: Up-regulated by cold treatment.
CC {ECO:0000269|PubMed:21632542}.
CC -!- PTM: Glutathionylated. {ECO:0000269|PubMed:21632542}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. CPYC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA22979.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035353; CAA22979.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161573; CAB81461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85535.1; -; Genomic_DNA.
DR EMBL; AK118672; BAC43267.1; -; mRNA.
DR EMBL; BT003703; AAO39931.1; -; mRNA.
DR PIR; T04526; T04526.
DR RefSeq; NP_194602.2; NM_119017.5.
DR PDB; 3RHB; X-ray; 1.20 A; A=64-174.
DR PDB; 3RHC; X-ray; 2.40 A; A/B=64-174.
DR PDBsum; 3RHB; -.
DR PDBsum; 3RHC; -.
DR AlphaFoldDB; Q8GWS0; -.
DR SMR; Q8GWS0; -.
DR BioGRID; 14281; 5.
DR IntAct; Q8GWS0; 2.
DR STRING; 3702.AT4G28730.1; -.
DR iPTMnet; Q8GWS0; -.
DR PaxDb; Q8GWS0; -.
DR PRIDE; Q8GWS0; -.
DR ProteomicsDB; 222279; -.
DR EnsemblPlants; AT4G28730.1; AT4G28730.1; AT4G28730.
DR GeneID; 828994; -.
DR Gramene; AT4G28730.1; AT4G28730.1; AT4G28730.
DR KEGG; ath:AT4G28730; -.
DR Araport; AT4G28730; -.
DR TAIR; locus:2117793; AT4G28730.
DR eggNOG; KOG1752; Eukaryota.
DR HOGENOM; CLU_026126_5_2_1; -.
DR InParanoid; Q8GWS0; -.
DR OMA; GVEPMVI; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q8GWS0; -.
DR EvolutionaryTrace; Q8GWS0; -.
DR PRO; PR:Q8GWS0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWS0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IDA:TAIR.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:TAIR.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chloroplast; Disulfide bond; Electron transport;
KW Glutathionylation; Plastid; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:22223895"
FT CHAIN 52..174
FT /note="Glutaredoxin-C5, chloroplastic"
FT /id="PRO_0000268712"
FT DOMAIN 93..171
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 135
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21632542"
FT BINDING 148
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21632542"
FT BINDING 149
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:21632542"
FT MOD_RES 52
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 90
FT /note="S-glutathionyl cysteine; partial"
FT /evidence="ECO:0000269|PubMed:21632542"
FT MOD_RES 148
FT /note="S-glutathionyl cysteine; partial"
FT /evidence="ECO:0000269|PubMed:21632542"
FT DISULFID 90..93
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P25373"
FT MUTAGEN 90
FT /note="C->S: Loss of Fe-S cluster incorporation and loss of
FT glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:21632542"
FT MUTAGEN 93
FT /note="C->S: Loss of Fe-S cluster incorporation, but
FT increased glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:21632542"
FT MUTAGEN 141
FT /note="C->S: No effect on Fe-S cluster incorporation or on
FT glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:21632542"
FT MUTAGEN 148
FT /note="C->S: No effect on Fe-S cluster incorporation or on
FT glutaredoxin activity."
FT /evidence="ECO:0000269|PubMed:21632542"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:3RHB"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:3RHB"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:3RHB"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3RHB"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3RHB"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:3RHB"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:3RHB"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:3RHB"
FT HELIX 148..156
FT /evidence="ECO:0007829|PDB:3RHB"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:3RHB"
SQ 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
