Entry euk: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   10-MAY-2017, entry version 87.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   Fe-S 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
RT   in 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,
RP   AND GLUTATHIONYLATION AT CYS-131.
RX   PubMed=24203231; DOI=10.1093/mp/sst156;
RA   Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D.,
RA   Gualberto J.M., Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
RT   "Monothiol glutaredoxin-BolA interactions: redox control of
RT   Arabidopsis 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
RT   complexes.";
RL   J. Biol. Chem. 289:24588-24598(2014).
CC   -!- FUNCTION: Participates in cysteine desulfurization mediated by
CC       NFS2 in chloroplast and NIFS1 in mitochondrion (PubMed:16437155).
CC       Activates the cysteine desulfurase activity of NFS2
CC       (PubMed:16455656). Cysteine desulfurization mobilizes sulfur from
CC       L-cysteine to yield L-alanine and supplies the inorganic sulfur
CC       for iron-sulfur (Fe-S) cluster formation. Glutaredoxins regulate
CC       SUFE1 activity by inducing its reduction and deglutathionylation
CC       (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
CC       with NFS2 and NIFS1 (PubMed:16437155). Interacts in vitro with
CC       GRXS14, GRXS15, GRXS16 and GRXS17, but not with GRXC5
CC       (PubMed:24203231). Interacts in vivo only with GRXS14 and GRXS16
CC       (PubMed:24203231). {ECO:0000269|PubMed:16437155,
CC       ECO:0000269|PubMed:16455656, 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
CC       and chlorosis. {ECO:0000305|PubMed:16437155}.
CC   -!- SIMILARITY: Belongs to the SufE family. {ECO:0000305}.
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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   UniGene; At.32175; -.
DR   PDB; 4PUI; X-ray; 1.70 A; A/B=277-371.
DR   PDBsum; 4PUI; -.
DR   ProteinModelPortal; Q84W65; -.
DR   SMR; Q84W65; -.
DR   BioGrid; 14043; 6.
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   OMA; FQSVPDP; -.
DR   OrthoDB; EOG09360VRW; -.
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:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR   InterPro; IPR002634; BolA.
DR   InterPro; IPR003808; Fe-S_metab-assoc_dom.
DR   PANTHER; PTHR12735; PTHR12735; 1.
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; Complete proteome; Glutathionylation;
KW   Mitochondrion; Plastid; Reference proteome; Transit peptide.
FT   TRANSIT       1     66       Chloroplast and mitochondrion.
FT                                {ECO:0000305}.
FT   CHAIN        67    371       SufE-like protein 1,
FT                                chloroplastic/mitochondrial.
FT                                /FTId=PRO_0000250653.
FT   ACT_SITE    131    131       Cysteine persulfide intermediate.
FT                                {ECO:0000250}.
FT   MOD_RES     131    131       S-glutathionyl cysteine.
FT                                {ECO:0000305|PubMed:24203231}.
FT   MUTAGEN     131    131       C->S: Loss of function.
FT                                {ECO:0000269|PubMed:16455656}.
FT   CONFLICT    160    160       G -> R (in Ref. 3; AAO42209).
FT                                {ECO:0000305}.
FT   HELIX       280    293       {ECO:0000244|PDB:4PUI}.
FT   STRAND      296    302       {ECO:0000244|PDB:4PUI}.
FT   HELIX       304    306       {ECO:0000244|PDB:4PUI}.
FT   STRAND      324    330       {ECO:0000244|PDB:4PUI}.
FT   HELIX       332    334       {ECO:0000244|PDB:4PUI}.
FT   HELIX       339    349       {ECO:0000244|PDB:4PUI}.
FT   HELIX       351    354       {ECO:0000244|PDB:4PUI}.
FT   TURN        355    357       {ECO:0000244|PDB:4PUI}.
FT   STRAND      360    366       {ECO:0000244|PDB:4PUI}.
FT   HELIX       368    370       {ECO:0000244|PDB:4PUI}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        92    211       ipfam:SufE [T]
FT   MYHIT       289    370       ipfam:BolA [T]
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
//