Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cysteine desulfurase 1, chloroplastic

Gene

NFS2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine (PubMed:12033984, PubMed:16455656). Supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters (PubMed:15480755, PubMed:17372218). Required for the maturation of all plastidic Fe-S proteins and, thus, essential for plant growth (PubMed:17372218).4 Publications

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.4 Publications
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.2 Publications

Cofactori

Enzyme regulationi

The cysteine desulfurase activity is stimulated over 40-fold upon complex formation with SUFE1 (PubMed:16437155, PubMed:16455656).2 Publications

Kineticsi

  1. KM=0.11 mM for L-Cysteine (at 37 degrees Celsius and pH 7.9)1 Publication
  2. KM=2.7 mM for L-Selenocysteine (at 37 degrees Celsius and pH 7.9)1 Publication
  1. Vmax=0.0013 µmol/min/mg enzyme with L-cysteine as substrate1 Publication
  2. Vmax=2.44 µmol/min/mg enzyme with L-Selenocysteine as substrate1 Publication

pH dependencei

Optimum pH is 7-9.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei418 – 4181Cysteine persulfide intermediateBy similarity

GO - Molecular functioni

  • cysteine desulfurase activity Source: TAIR
  • pyridoxal phosphate binding Source: InterPro
  • selenocysteine lyase activity Source: TAIR

GO - Biological processi

  • cysteine metabolic process Source: InterPro
  • iron incorporation into metallo-sulfur cluster Source: TAIR
  • response to selenium ion Source: TAIR
  • selenium compound metabolic process Source: TAIR
  • sulfur compound metabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.8.1.7. 399.
SABIO-RKQ93WX6.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine desulfurase 1, chloroplastic1 Publication (EC:2.8.1.74 Publications)
Alternative name(s):
NIFS-like protein 11 Publication
Short name:
CpNifS1
Plastid sufS-like protein
Protein AtCpNifS
Selenocysteine lyase (EC:4.4.1.162 Publications)
Gene namesi
Name:NFS21 Publication
Synonyms:CpNIFS1 Publication, CpNIFS1
Ordered Locus Names:At1g08490Imported
ORF Names:T27G7.17Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G08490.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Biotechnological usei

NFS2-overexpressing transgenic plants have enhanced ability to tolerate and accumulate Se and may be used in phytoremediation.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi388 – 3881C → S: Total loss of the Cys desulfurase activity, but only 20% decrease of the SeCys lyase activity. 1 Publication
Mutagenesisi418 – 4181C → S: Loss of catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535ChloroplastAdd
BLAST
Chaini36 – 463428Cysteine desulfurase 1, chloroplasticPRO_0000250652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiQ93WX6.
PRIDEiQ93WX6.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

GenevisibleiQ93WX6. AT.

Interactioni

Subunit structurei

Heterotetramer with SUFE1 (PubMed:16455656). Interacts with QS (PubMed:18978034). Interacts with SUFE1 (PubMed:16437155, PubMed:18978034).3 Publications

Protein-protein interaction databases

BioGridi22611. 2 interactions.
STRINGi3702.AT1G08490.1.

Structurei

Secondary structure

1
463
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 575Combined sources
Helixi58 – 603Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 684Combined sources
Turni78 – 803Combined sources
Helixi86 – 9813Combined sources
Helixi109 – 12820Combined sources
Helixi134 – 1363Combined sources
Beta strandi137 – 1426Combined sources
Helixi143 – 15311Combined sources
Helixi155 – 1584Combined sources
Beta strandi164 – 1685Combined sources
Helixi173 – 18614Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi199 – 2013Combined sources
Helixi203 – 2075Combined sources
Beta strandi214 – 2229Combined sources
Turni224 – 2263Combined sources
Helixi232 – 2409Combined sources
Turni241 – 2433Combined sources
Beta strandi245 – 2495Combined sources
Turni251 – 2566Combined sources
Helixi261 – 2644Combined sources
Beta strandi267 – 2726Combined sources
Helixi273 – 2753Combined sources
Beta strandi283 – 2875Combined sources
Helixi289 – 2946Combined sources
Beta strandi301 – 3088Combined sources
Beta strandi313 – 3153Combined sources
Helixi320 – 3223Combined sources
Helixi329 – 34517Combined sources
Helixi347 – 36620Combined sources
Beta strandi371 – 3733Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi386 – 3927Combined sources
Helixi397 – 40812Combined sources
Beta strandi413 – 4153Combined sources
Helixi420 – 4256Combined sources
Beta strandi431 – 4355Combined sources
Helixi442 – 46019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q75X-ray1.71A/B36-463[»]
4Q76X-ray1.90A/B36-463[»]
ProteinModelPortaliQ93WX6.
SMRiQ93WX6. Positions 51-463.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410INGQ. Eukaryota.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiQ93WX6.
KOiK11717.
OMAiMIDFVGL.
PhylomeDBiQ93WX6.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR010970. Cys_dSase_SufS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01979. sufS. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q93WX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGVAMKLPS FPNAISIGHR SFSRVRCSSS LSVCSAAAAS SATISTDSES
60 70 80 90 100
VSLGHRVRKD FRILHQEVNG SKLVYLDSAA TSQKPAAVLD ALQNYYEFYN
110 120 130 140 150
SNVHRGIHYL SAKATDEFEL ARKKVARFIN ASDSREIVFT RNATEAINLV
160 170 180 190 200
AYSWGLSNLK PGDEVILTVA EHHSCIVPWQ IVSQKTGAVL KFVTLNEDEV
210 220 230 240 250
PDINKLRELI SPKTKLVAVH HVSNVLASSL PIEEIVVWAH DVGAKVLVDA
260 270 280 290 300
CQSVPHMVVD VQKLNADFLV ASSHKMCGPT GIGFLYGKSD LLHSMPPFLG
310 320 330 340 350
GGEMISDVFL DHSTYAEPPS RFEAGTPAIG EAIALGAAVD YLSGIGMPKI
360 370 380 390 400
HEYEVEIGKY LYEKLSSLPD VRIYGPRPSE SVHRGALCSF NVEGLHPTDL
410 420 430 440 450
ATFLDQQHGV AIRSGHHCAQ PLHRYLGVNA SARASLYFYN TKDDVDAFIV
460
ALADTVSFFN SFK
Length:463
Mass (Da):50,485
Last modified:December 1, 2001 - v1
Checksum:i7A00460377E01067
GO

Sequence cautioni

The sequence AAF22900.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY078068 mRNA. Translation: AAL79956.1.
AF419347 mRNA. Translation: AAL14994.1.
AC006932 Genomic DNA. Translation: AAF22900.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28298.1.
AY094425 mRNA. Translation: AAM19798.1.
AY149950 mRNA. Translation: AAN31104.1.
RefSeqiNP_172325.2. NM_100722.4.
UniGeneiAt.22935.
At.26502.

Genome annotation databases

EnsemblPlantsiAT1G08490.1; AT1G08490.1; AT1G08490.
GeneIDi837370.
GrameneiAT1G08490.1; AT1G08490.1; AT1G08490.
KEGGiath:AT1G08490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY078068 mRNA. Translation: AAL79956.1.
AF419347 mRNA. Translation: AAL14994.1.
AC006932 Genomic DNA. Translation: AAF22900.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28298.1.
AY094425 mRNA. Translation: AAM19798.1.
AY149950 mRNA. Translation: AAN31104.1.
RefSeqiNP_172325.2. NM_100722.4.
UniGeneiAt.22935.
At.26502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q75X-ray1.71A/B36-463[»]
4Q76X-ray1.90A/B36-463[»]
ProteinModelPortaliQ93WX6.
SMRiQ93WX6. Positions 51-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22611. 2 interactions.
STRINGi3702.AT1G08490.1.

Proteomic databases

PaxDbiQ93WX6.
PRIDEiQ93WX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G08490.1; AT1G08490.1; AT1G08490.
GeneIDi837370.
GrameneiAT1G08490.1; AT1G08490.1; AT1G08490.
KEGGiath:AT1G08490.

Organism-specific databases

TAIRiAT1G08490.

Phylogenomic databases

eggNOGiENOG410INGQ. Eukaryota.
COG0520. LUCA.
HOGENOMiHOG000017511.
InParanoidiQ93WX6.
KOiK11717.
OMAiMIDFVGL.
PhylomeDBiQ93WX6.

Enzyme and pathway databases

BRENDAi2.8.1.7. 399.
SABIO-RKQ93WX6.

Miscellaneous databases

PROiQ93WX6.

Gene expression databases

GenevisibleiQ93WX6. AT.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR010970. Cys_dSase_SufS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01979. sufS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase."
    Leon S., Touraine B., Briat J.-F., Lobreaux S.
    Biochem. J. 366:557-564(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR.
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Characterization of a NifS-like chloroplast protein from Arabidopsis. Implications for its role in sulfur and selenium metabolism."
    Pilon-Smits E.A.H., Garifullina G.F., Abdel-Ghany S., Kato S., Mihara H., Hale K.L., Burkhead J.L., Esaki N., Kurihara T., Pilon M.
    Plant Physiol. 130:1309-1318(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: cv. Columbia.
    Tissue: Seedling.
  3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "The chloroplast NifS-like protein of Arabidopsis thaliana is required for iron-sulfur cluster formation in ferredoxin."
    Ye H., Garifullina G.F., Abdel-Ghany S.E., Zhang L., Pilon-Smits E.A., Pilon M.
    Planta 220:602-608(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-418, SUBCELLULAR LOCATION.
  7. Cited for: SUBCELLULAR LOCATION, BIOTECHNOLOGY.
  8. "AtSufE is an essential activator of plastidic and mitochondrial desulfurases in Arabidopsis."
    Xu X.M., Moeller S.G.
    EMBO J. 25:900-909(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SUFE1.
  9. "CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation."
    Ye H., Abdel-Ghany S.E., Anderson T.D., Pilon-Smits E.A., Pilon M.
    J. Biol. Chem. 281:8958-8969(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INTERACTION WITH SUFE1, SUBUNIT, MUTAGENESIS OF CYS-388.
  10. "Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS."
    Van Hoewyk D., Abdel-Ghany S.E., Cohu C.M., Herbert S.K., Kugrens P., Pilon M., Pilon-Smits E.A.
    Proc. Natl. Acad. Sci. U.S.A. 104:5686-5691(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase affects nicotinamide adenine dinucleotide biosynthesis and causes early ageing."
    Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R., Dijkwel P.P.
    Plant Cell 20:2909-2925(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH QS AND SUFE1.
    Strain: cv. Landsberg erecta.
  12. "Structural and functional studies of the mitochondrial cysteine desulfurase from Arabidopsis thaliana."
    Turowski V.R., Busi M.V., Gomez-Casati D.F.
    Mol. Plant 5:1001-1010(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiCNIF1_ARATH
AccessioniPrimary (citable) accession number: Q93WX6
Secondary accession number(s): Q9SJE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: December 1, 2001
Last modified: February 17, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.