CNIF1_ARATH
ID CNIF1_ARATH Reviewed; 463 AA.
AC Q93WX6; Q9SJE3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Cysteine desulfurase 1, chloroplastic {ECO:0000303|PubMed:12033984};
DE EC=2.8.1.7 {ECO:0000269|PubMed:12033984, ECO:0000269|PubMed:12427997, ECO:0000269|PubMed:15480755, ECO:0000269|PubMed:16455656};
DE AltName: Full=NIFS-like protein 1 {ECO:0000303|PubMed:12427997};
DE Short=CpNifS1;
DE AltName: Full=Plastid sufS-like protein;
DE AltName: Full=Protein AtCpNifS;
DE AltName: Full=Selenocysteine lyase;
DE EC=4.4.1.16 {ECO:0000269|PubMed:12427997, ECO:0000269|PubMed:16455656};
DE Flags: Precursor;
GN Name=NFS2 {ECO:0000303|PubMed:12033984};
GN Synonyms=CpNIFS {ECO:0000303|PubMed:17372218}, CpNIFS1;
GN OrderedLocusNames=At1g08490 {ECO:0000312|Araport:AT1G08490};
GN ORFNames=T27G7.17 {ECO:0000312|EMBL:AAF22900.1};
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=12033984; DOI=10.1042/bj20020322;
RA Leon S., Touraine B., Briat J.-F., Lobreaux S.;
RT "The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial
RT cysteine desulphurase.";
RL Biochem. J. 366:557-564(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=12427997; DOI=10.1104/pp.102.010280;
RA Pilon-Smits E.A.H., Garifullina G.F., Abdel-Ghany S., Kato S., Mihara H.,
RA Hale K.L., Burkhead J.L., Esaki N., Kurihara T., Pilon M.;
RT "Characterization of a NifS-like chloroplast protein from Arabidopsis.
RT Implications for its role in sulfur and selenium metabolism.";
RL Plant Physiol. 130:1309-1318(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-418, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15480755; DOI=10.1007/s00425-004-1388-1;
RA Ye H., Garifullina G.F., Abdel-Ghany S.E., Zhang L., Pilon-Smits E.A.,
RA Pilon M.;
RT "The chloroplast NifS-like protein of Arabidopsis thaliana is required for
RT iron-sulfur cluster formation in ferredoxin.";
RL Planta 220:602-608(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=16244144; DOI=10.1104/pp.105.068684;
RA Van Hoewyk D., Garifullina G.F., Ackley A.R., Abdel-Ghany S.E.,
RA Marcus M.A., Fakra S., Ishiyama K., Inoue E., Pilon M., Takahashi H.,
RA Pilon-Smits E.A.;
RT "Overexpression of AtCpNifS enhances selenium tolerance and accumulation in
RT Arabidopsis.";
RL Plant Physiol. 139:1518-1528(2005).
RN [8]
RP ACTIVITY REGULATION, AND INTERACTION WITH SUFE1.
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, INTERACTION WITH SUFE1, SUBUNIT, AND MUTAGENESIS OF CYS-388.
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 [10]
RP FUNCTION.
RX PubMed=17372218; DOI=10.1073/pnas.0700774104;
RA Van Hoewyk D., Abdel-Ghany S.E., Cohu C.M., Herbert S.K., Kugrens P.,
RA Pilon M., Pilon-Smits E.A.;
RT "Chloroplast iron-sulfur cluster protein maturation requires the essential
RT cysteine desulfurase CpNifS.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5686-5691(2007).
RN [11]
RP INTERACTION WITH QS AND SUFE1.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18978034; DOI=10.1105/tpc.107.056341;
RA Schippers J.H., Nunes-Nesi A., Apetrei R., Hille J., Fernie A.R.,
RA Dijkwel P.P.;
RT "The Arabidopsis onset of leaf death5 mutation of quinolinate synthase
RT affects nicotinamide adenine dinucleotide biosynthesis and causes early
RT ageing.";
RL Plant Cell 20:2909-2925(2008).
RN [12]
RP 3D-STRUCTURE MODELING.
RX PubMed=22511606; DOI=10.1093/mp/sss037;
RA Turowski V.R., Busi M.V., Gomez-Casati D.F.;
RT "Structural and functional studies of the mitochondrial cysteine
RT desulfurase from Arabidopsis thaliana.";
RL Mol. Plant 5:1001-1010(2012).
CC -!- FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms
CC from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to
CC produce L-alanine (PubMed:12033984, PubMed:16455656). Supplies the
CC inorganic sulfur for iron-sulfur (Fe-S) clusters (PubMed:15480755,
CC PubMed:17372218). Required for the maturation of all plastidic Fe-S
CC proteins and, thus, essential for plant growth (PubMed:17372218).
CC {ECO:0000269|PubMed:12033984, ECO:0000269|PubMed:15480755,
CC ECO:0000269|PubMed:16455656, ECO:0000269|PubMed:17372218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:12033984,
CC ECO:0000269|PubMed:12427997, ECO:0000269|PubMed:15480755,
CC ECO:0000269|PubMed:16455656};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16;
CC Evidence={ECO:0000269|PubMed:12427997, ECO:0000269|PubMed:16455656};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: The cysteine desulfurase activity is stimulated
CC over 40-fold upon complex formation with SUFE1 (PubMed:16437155,
CC PubMed:16455656). {ECO:0000269|PubMed:16437155,
CC ECO:0000269|PubMed:16455656}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for L-Cysteine (at 37 degrees Celsius and pH 7.9)
CC {ECO:0000269|PubMed:12427997};
CC KM=2.7 mM for L-Selenocysteine (at 37 degrees Celsius and pH 7.9)
CC {ECO:0000269|PubMed:12427997};
CC Vmax=0.0013 umol/min/mg enzyme with L-cysteine as substrate
CC {ECO:0000269|PubMed:16455656};
CC Vmax=2.44 umol/min/mg enzyme with L-Selenocysteine as substrate
CC {ECO:0000269|PubMed:16455656};
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:12427997};
CC -!- SUBUNIT: Heterotetramer with SUFE1 (PubMed:16455656). Interacts with QS
CC (PubMed:18978034). Interacts with SUFE1 (PubMed:16437155,
CC PubMed:18978034). {ECO:0000269|PubMed:16437155,
CC ECO:0000269|PubMed:16455656, ECO:0000269|PubMed:18978034}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:12033984, ECO:0000269|PubMed:12427997,
CC ECO:0000269|PubMed:16244144}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:15480755}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12033984,
CC ECO:0000269|PubMed:12427997}.
CC -!- BIOTECHNOLOGY: NFS2-overexpressing transgenic plants have enhanced
CC ability to tolerate and accumulate Se and may be used in
CC phytoremediation. {ECO:0000269|PubMed:16244144}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY078068; AAL79956.1; -; mRNA.
DR EMBL; AF419347; AAL14994.1; -; mRNA.
DR EMBL; AC006932; AAF22900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28298.1; -; Genomic_DNA.
DR EMBL; AY094425; AAM19798.1; -; mRNA.
DR EMBL; AY149950; AAN31104.1; -; mRNA.
DR RefSeq; NP_172325.2; NM_100722.5.
DR PDB; 4Q75; X-ray; 1.71 A; A/B=36-463.
DR PDB; 4Q76; X-ray; 1.90 A; A/B=36-463.
DR PDBsum; 4Q75; -.
DR PDBsum; 4Q76; -.
DR AlphaFoldDB; Q93WX6; -.
DR SMR; Q93WX6; -.
DR BioGRID; 22611; 2.
DR STRING; 3702.AT1G08490.1; -.
DR PaxDb; Q93WX6; -.
DR PRIDE; Q93WX6; -.
DR ProteomicsDB; 241244; -.
DR EnsemblPlants; AT1G08490.1; AT1G08490.1; AT1G08490.
DR GeneID; 837370; -.
DR Gramene; AT1G08490.1; AT1G08490.1; AT1G08490.
DR KEGG; ath:AT1G08490; -.
DR Araport; AT1G08490; -.
DR TAIR; locus:2201856; AT1G08490.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_2_5_1; -.
DR InParanoid; Q93WX6; -.
DR OMA; HKLCGPT; -.
DR OrthoDB; 697150at2759; -.
DR PhylomeDB; Q93WX6; -.
DR BRENDA; 2.8.1.7; 399.
DR SABIO-RK; Q93WX6; -.
DR PRO; PR:Q93WX6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93WX6; baseline and differential.
DR Genevisible; Q93WX6; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0031071; F:cysteine desulfurase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009000; F:selenocysteine lyase activity; IDA:TAIR.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR GO; GO:0018283; P:iron incorporation into metallo-sulfur cluster; IDA:TAIR.
DR GO; GO:0010269; P:response to selenium ion; IMP:TAIR.
DR GO; GO:0001887; P:selenium compound metabolic process; IDA:TAIR.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:TAIR.
DR CDD; cd06453; SufS_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01979; sufS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Lyase; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT CHAIN 36..463
FT /note="Cysteine desulfurase 1, chloroplastic"
FT /id="PRO_0000250652"
FT ACT_SITE 418
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 275
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 388
FT /note="C->S: Total loss of the Cys desulfurase activity,
FT but only 20% decrease of the SeCys lyase activity."
FT /evidence="ECO:0000269|PubMed:16455656"
FT MUTAGEN 418
FT /note="C->S: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:15480755"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4Q75"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 109..128
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:4Q75"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 232..240
FT /evidence="ECO:0007829|PDB:4Q75"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4Q75"
FT TURN 251..256
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 261..264
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 347..366
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4Q76"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 397..408
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 420..425
FT /evidence="ECO:0007829|PDB:4Q75"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:4Q75"
FT HELIX 442..460
FT /evidence="ECO:0007829|PDB:4Q75"
SQ SEQUENCE 463 AA; 50485 MW; 7A00460377E01067 CRC64;
MEGVAMKLPS FPNAISIGHR SFSRVRCSSS LSVCSAAAAS SATISTDSES VSLGHRVRKD
FRILHQEVNG SKLVYLDSAA TSQKPAAVLD ALQNYYEFYN SNVHRGIHYL SAKATDEFEL
ARKKVARFIN ASDSREIVFT RNATEAINLV AYSWGLSNLK PGDEVILTVA EHHSCIVPWQ
IVSQKTGAVL KFVTLNEDEV PDINKLRELI SPKTKLVAVH HVSNVLASSL PIEEIVVWAH
DVGAKVLVDA CQSVPHMVVD VQKLNADFLV ASSHKMCGPT GIGFLYGKSD LLHSMPPFLG
GGEMISDVFL DHSTYAEPPS RFEAGTPAIG EAIALGAAVD YLSGIGMPKI HEYEVEIGKY
LYEKLSSLPD VRIYGPRPSE SVHRGALCSF NVEGLHPTDL ATFLDQQHGV AIRSGHHCAQ
PLHRYLGVNA SARASLYFYN TKDDVDAFIV ALADTVSFFN SFK
