(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 99.
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}.
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   SMR; Q84W65; -.
DR   BioGrid; 14043; 9.
DR   STRING; 3702.AT4G26500.1; -.
DR   iPTMnet; Q84W65; -.
DR   SwissPalm; Q84W65; -.
DR   PaxDb; Q84W65; -.
DR   PRIDE; Q84W65; -.
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; ENOG410J25M; Eukaryota.
DR   eggNOG; KOG2313; Eukaryota.
DR   eggNOG; COG0271; LUCA.
DR   eggNOG; COG2166; LUCA.
DR   HOGENOM; HOG000241241; -.
DR   InParanoid; Q84W65; -.
DR   KO; K22066; -.
DR   OMA; FQSVPDP; -.
DR   OrthoDB; 929897at2759; -.
DR   PhylomeDB; Q84W65; -.
DR   UniPathway; UPA00266; -.
DR   PRO; PR:Q84W65; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q84W65; baseline and 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   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;
DR   PRODOM; Q84W65.
DR   SWISS-2DPAGE; Q84W65.
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   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:0000244|PDB:4PUI"
FT   STRAND          296..302
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   HELIX           304..306
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   STRAND          324..330
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   HELIX           332..334
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   HELIX           339..349
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   HELIX           351..354
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   TURN            355..357
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   STRAND          360..366
FT                   /evidence="ECO:0000244|PDB:4PUI"
FT   HELIX           368..370
FT                   /evidence="ECO:0000244|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
//

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