SUFE1_ARATH
ID SUFE1_ARATH Reviewed; 371 AA.
AC Q84W65; O65584;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=SufE-like protein 1, chloroplastic/mitochondrial {ECO:0000303|PubMed:17452319};
DE AltName: Full=Chloroplastic SufE {ECO:0000303|PubMed:16455656};
DE Short=CpSufE {ECO:0000303|PubMed:16455656};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1374;
DE AltName: Full=Protein SULFUR E {ECO:0000303|PubMed:16437155};
DE Short=AtSUFE {ECO:0000303|PubMed:16437155};
DE AltName: Full=Protein SULFUR E 1 {ECO:0000303|PubMed:17452319};
DE Short=AtSUFE1 {ECO:0000303|PubMed:17452319};
DE Flags: Precursor;
GN Name=SUFE1 {ECO:0000303|PubMed:17452319};
GN Synonyms=EMB1374, SUFE {ECO:0000303|PubMed:16437155,
GN ECO:0000303|PubMed:16455656}; OrderedLocusNames=At4g26500;
GN ORFNames=M3E9.70;
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, INTERACTION WITH NFS2 AND NIFS1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16437155; DOI=10.1038/sj.emboj.7600968;
RA Xu X.M., Moeller S.G.;
RT "AtSufE is an essential activator of plastidic and mitochondrial
RT desulfurases in Arabidopsis.";
RL EMBO J. 25:900-909(2006).
RN [7]
RP FUNCTION, INTERACTION WITH NFS2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-131.
RX PubMed=16455656; DOI=10.1074/jbc.m512737200;
RA Ye H., Abdel-Ghany S.E., Anderson T.D., Pilon-Smits E.A., Pilon M.;
RT "CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S
RT cluster formation.";
RL J. Biol. Chem. 281:8958-8969(2006).
RN [8]
RP GENE FAMILY.
RX PubMed=17452319; DOI=10.1074/jbc.m701428200;
RA Narayana Murthy U.M., Ollagnier-de-Choudens S., Sanakis Y.,
RA Abdel-Ghany S.E., Rousset C., Ye H., Fontecave M., Pilon-Smits E.A.,
RA Pilon M.;
RT "Characterization of Arabidopsis thaliana SufE2 and SufE3: functions in
RT chloroplast iron-sulfur cluster assembly and Nad synthesis.";
RL J. Biol. Chem. 282:18254-18264(2007).
RN [9]
RP FUNCTION, INTERACTION WITH GRXC5; GRXS14; GRXS15; GRXS16 AND GRXS17, AND
RP GLUTATHIONYLATION AT CYS-131.
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 277-371.
RX PubMed=25012657; DOI=10.1074/jbc.m114.572701;
RA Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N.,
RA Didierjean C.;
RT "Structural and spectroscopic insights into BolA-glutaredoxin complexes.";
RL J. Biol. Chem. 289:24588-24598(2014).
CC -!- FUNCTION: Participates in cysteine desulfurization mediated by NFS2 in
CC chloroplast and NIFS1 in mitochondrion (PubMed:16437155). Activates the
CC cysteine desulfurase activity of NFS2 (PubMed:16455656). Cysteine
CC desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and
CC supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation.
CC Glutaredoxins regulate SUFE1 activity by inducing its reduction and
CC deglutathionylation (PubMed:24203231). {ECO:0000269|PubMed:16437155,
CC ECO:0000269|PubMed:16455656, ECO:0000269|PubMed:24203231}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: Heterotetramer with NFS2 (PubMed:16455656). Interacts with
CC NFS2 and NIFS1 (PubMed:16437155). Interacts in vitro with GRXS14,
CC GRXS15, GRXS16 and GRXS17, but not with GRXC5 (PubMed:24203231).
CC Interacts in vivo only with GRXS14 and GRXS16 (PubMed:24203231).
CC {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:16455656,
CC ECO:0000269|PubMed:24203231}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:16455656}.
CC Mitochondrion {ECO:0000269|PubMed:16437155}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:16455656}.
CC -!- PTM: Glutathionylated. Glutathionylation strongly reduces the
CC stimulation of NFS2 activity. {ECO:0000269|PubMed:24203231}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:16437155}.
CC -!- MISCELLANEOUS: Over-expression of SUFE1 leads to retarded growth and
CC chlorosis. {ECO:0000305|PubMed:16437155}.
CC -!- SIMILARITY: Belongs to the SufE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL022223; CAA18220.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79505.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85210.1; -; Genomic_DNA.
DR EMBL; BT004190; AAO42209.1; -; mRNA.
DR EMBL; BT021125; AAX22260.1; -; mRNA.
DR EMBL; AY084591; AAM61156.1; -; mRNA.
DR PIR; T05054; T05054.
DR RefSeq; NP_194380.1; NM_118783.3.
DR PDB; 4PUI; X-ray; 1.70 A; A/B=277-371.
DR PDBsum; 4PUI; -.
DR AlphaFoldDB; Q84W65; -.
DR SMR; Q84W65; -.
DR BioGRID; 14043; 9.
DR STRING; 3702.AT4G26500.1; -.
DR iPTMnet; Q84W65; -.
DR SwissPalm; Q84W65; -.
DR PaxDb; Q84W65; -.
DR PRIDE; Q84W65; -.
DR ProteomicsDB; 228280; -.
DR EnsemblPlants; AT4G26500.1; AT4G26500.1; AT4G26500.
DR GeneID; 828756; -.
DR Gramene; AT4G26500.1; AT4G26500.1; AT4G26500.
DR KEGG; ath:AT4G26500; -.
DR Araport; AT4G26500; -.
DR TAIR; locus:2131488; AT4G26500.
DR eggNOG; KOG2313; Eukaryota.
DR HOGENOM; CLU_041968_0_0_1; -.
DR InParanoid; Q84W65; -.
DR OMA; FQSVPDP; -.
DR PhylomeDB; Q84W65; -.
DR UniPathway; UPA00266; -.
DR PRO; PR:Q84W65; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84W65; differential.
DR Genevisible; Q84W65; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR Pfam; PF01722; BolA; 1.
DR Pfam; PF02657; SufE; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Glutathionylation; Mitochondrion; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN 67..371
FT /note="SufE-like protein 1, chloroplastic/mitochondrial"
FT /id="PRO_0000250653"
FT REGION 218..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000305|PubMed:24203231"
FT MUTAGEN 131
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:16455656"
FT CONFLICT 160
FT /note="G -> R (in Ref. 3; AAO42209)"
FT /evidence="ECO:0000305"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:4PUI"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:4PUI"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4PUI"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:4PUI"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:4PUI"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4PUI"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:4PUI"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4PUI"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:4PUI"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4PUI"
SQ SEQUENCE 371 AA; 40834 MW; 1843F0670DC057C3 CRC64;
MAAAMSSSCC ASSLRLIPFK RTLFSSIHYP AKTLLLRPLK PSEVPSFRRT IITFQKISTG
IVPPPSASSS PSSYGDLQPI EELPPKLQEI VKLFQSVQEP KAKYEQLMFY GKNLTPLDSQ
FKTRENKVEG CVSQVWVRAF FDEERNVVYE ADSDSVLTKG LAALLVKGLS GRPVPEILRI
TPDFAVLLGL QQSLSPSRNN GLLNMLKLMQ KKALHLEVKG EEDSSSGESS ESSFVSIPET
KDEANVPEVD LESKPDLVED LGTEKIDDSE SGSNVVALGS RGMRIREKLE KELDPVELEV
EDVSYQHAGH AAVRGSAGDD GETHFNLRIV SDAFQGKSLV KRHRLIYDLL QDELKSGLHA
LSIVAKTPAE V
