CYSD1_ARATH
ID CYSD1_ARATH Reviewed; 324 AA.
AC Q9S6Z7; Q8LAQ6; Q9CAV8;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1;
DE EC=2.5.1.47 {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
DE EC=4.4.1.9 {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
DE AltName: Full=Beta-substituted Ala synthase 4;1;
DE Short=ARAth-Bsas4;1;
DE AltName: Full=Cysteine synthase D1;
DE Short=AtcysD1;
DE AltName: Full=O-acetylserine (thiol)-lyase 3;
GN Name=CYSD1; Synonyms=OAS3; OrderedLocusNames=At3g04940; ORFNames=T9J14.11;
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], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10845460; DOI=10.1093/pcp/41.4.465;
RA Yamaguchi Y., Nakamura T., Kusano T., Sano H.;
RT "Three Arabidopsis genes encoding proteins with differential activities for
RT cysteine synthase and beta-cyanoalanine synthase.";
RL Plant Cell Physiol. 41:465-476(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=10889265; DOI=10.1104/pp.123.3.1163;
RA Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
RT "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
RT protein in spinach and Arabidopsis.";
RL Plant Physiol. 123:1163-1171(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [7]
RP REVIEW.
RX PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
RA Wirtz M., Droux M.;
RT "Synthesis of the sulfur amino acids: cysteine and methionine.";
RL Photosyn. Res. 86:345-362(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=18223034; DOI=10.1105/tpc.107.056747;
RA Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M., Hell R.;
RT "Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
RT demonstrates compartment-specific differences in the regulation of cysteine
RT synthesis.";
RL Plant Cell 20:168-185(2008).
RN [9]
RP GENE FAMILY, AND DISRUPTION PHENOTYPE.
RX PubMed=18024555; DOI=10.1104/pp.107.106831;
RA Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
RT "Physiological roles of the beta-substituted alanine synthase gene family
RT in Arabidopsis.";
RL Plant Physiol. 146:310-320(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
RA Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
RT "Enzymes of cysteine synthesis show extensive and conserved modifications
RT patterns that include N(alpha)-terminal acetylation.";
RL Amino Acids 39:1077-1086(2010).
CC -!- FUNCTION: Acts as a cysteine synthase. The cysteine synthesis reaction
CC is more efficient than the cyanoalanine synthase activity.
CC {ECO:0000269|PubMed:18223034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC Evidence={ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + L-cysteine = 3-cyano-L-alanine + H(+) +
CC hydrogen sulfide; Xref=Rhea:RHEA:17821, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18407, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:77860; EC=4.4.1.9; Evidence={ECO:0000269|PubMed:10845460,
CC ECO:0000269|PubMed:10889265};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.69 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10889265};
CC KM=4.51 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10845460};
CC KM=4.98 mM for Na(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10889265};
CC KM=0.07 mM for Na(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10845460};
CC Vmax=0.2 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10889265};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10845460}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in flowers.
CC {ECO:0000269|PubMed:10845460}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18024555}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51407.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024284; BAA78562.1; -; mRNA.
DR EMBL; AJ011603; CAB56637.1; -; mRNA.
DR EMBL; AC009465; AAG51407.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74161.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63824.1; -; Genomic_DNA.
DR EMBL; AY136420; AAM97086.1; -; mRNA.
DR EMBL; BT008721; AAP42734.1; -; mRNA.
DR EMBL; AY087675; AAM65212.1; -; mRNA.
DR PIR; T52609; T52609.
DR RefSeq; NP_001325893.1; NM_001337549.1.
DR RefSeq; NP_566243.1; NM_111366.4.
DR AlphaFoldDB; Q9S6Z7; -.
DR SMR; Q9S6Z7; -.
DR BioGRID; 4989; 2.
DR IntAct; Q9S6Z7; 1.
DR STRING; 3702.AT3G04940.1; -.
DR MetOSite; Q9S6Z7; -.
DR PaxDb; Q9S6Z7; -.
DR PRIDE; Q9S6Z7; -.
DR ProteomicsDB; 224701; -.
DR EnsemblPlants; AT3G04940.1; AT3G04940.1; AT3G04940.
DR EnsemblPlants; AT3G04940.2; AT3G04940.2; AT3G04940.
DR GeneID; 819654; -.
DR Gramene; AT3G04940.1; AT3G04940.1; AT3G04940.
DR Gramene; AT3G04940.2; AT3G04940.2; AT3G04940.
DR KEGG; ath:AT3G04940; -.
DR Araport; AT3G04940; -.
DR TAIR; locus:2114804; AT3G04940.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; Q9S6Z7; -.
DR OMA; PETHYRT; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; Q9S6Z7; -.
DR BioCyc; ARA:AT3G04940-MON; -.
DR SABIO-RK; Q9S6Z7; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:Q9S6Z7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S6Z7; baseline and differential.
DR Genevisible; Q9S6Z7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
DR GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:TAIR.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR005856; Cys_synth.
DR InterPro; IPR005859; CysK.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..324
FT /note="Bifunctional L-3-cyanoalanine synthase/cysteine
FT synthase D1"
FT /id="PRO_0000424458"
FT BINDING 80
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 184..188
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 142
FT /note="N -> T (in Ref. 6; AAM65212)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34294 MW; FF2DAA731F52154F CRC64;
MEEDRCSIKD DATQLIGNTP MVYLNNIVDG CVARIAAKLE MMEPCSSVKE RIAYGMIKDA
EDKGLITPGK STLIEATSGN TGIGLAFIGA AKGYKVVLTM PSSMSLERKI ILLALGAEVH
LTDPSKGVQG IIDKAEEICS KNPDSIMLEQ FKNPSNPQTH YRTTGPEIWR DSAGEVDILV
AGVGTGGTLS GSGRFLKEKN KDFKVYGVEP TESAVISGGK PGTHLIQGIG AGLIPDNLDF
NVLDEVIQVT SVEAIETAKL LALKEGLLVG ISSGAAAAAA IKVAKRPENA GKLIVVIFPS
GGERYLSTSL FESVRHEAEN LPIQ
