CYSD2_ARATH
ID CYSD2_ARATH Reviewed; 323 AA.
AC Q9SXS7; B9DHF3; Q8LEC3; Q9SMY4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2;
DE EC=2.5.1.47 {ECO:0000269|PubMed:10845460};
DE EC=4.4.1.9 {ECO:0000269|PubMed:10845460};
DE AltName: Full=Beta-substituted Ala synthase 4;2;
DE Short=ARAth-Bsas4;2;
DE AltName: Full=Cysteine synthase D2;
DE Short=AtcysD2;
DE AltName: Full=O-acetylserine (thiol)-lyase 6;
GN Name=CYSD2; Synonyms=OAS6; OrderedLocusNames=At5g28020; ORFNames=F15F15.90;
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, INDUCTION BY NITROGEN STARVATION, AND
RP 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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 148-323, AND NOMENCLATURE.
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 [8]
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 [9]
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 [10]
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 [11]
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};
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;
CC Evidence={ECO:0000269|PubMed:10845460};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.97 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10845460};
CC KM=0.25 mM for Na(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10845460};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SXS7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in leaves and flowers.
CC {ECO:0000269|PubMed:10845460}.
CC -!- INDUCTION: By nitrogen starvation. {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}.
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DR EMBL; AB024283; BAA78561.1; -; mRNA.
DR EMBL; AC007627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93759.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93760.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93761.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93762.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93764.1; -; Genomic_DNA.
DR EMBL; AF424598; AAL11592.1; -; mRNA.
DR EMBL; AY124831; AAM70540.1; -; mRNA.
DR EMBL; AK317505; BAH20170.1; -; mRNA.
DR EMBL; AY085504; AAM62728.1; -; mRNA.
DR EMBL; AJ011044; CAB55622.1; -; mRNA.
DR PIR; T52661; T52661.
DR RefSeq; NP_001031956.1; NM_001036879.2. [Q9SXS7-1]
DR RefSeq; NP_001031957.1; NM_001036880.3. [Q9SXS7-1]
DR RefSeq; NP_001078628.1; NM_001085159.1. [Q9SXS7-1]
DR RefSeq; NP_198154.1; NM_122685.3. [Q9SXS7-1]
DR RefSeq; NP_851087.1; NM_180756.3. [Q9SXS7-1]
DR AlphaFoldDB; Q9SXS7; -.
DR SMR; Q9SXS7; -.
DR BioGRID; 18146; 2.
DR IntAct; Q9SXS7; 1.
DR STRING; 3702.AT5G28020.1; -.
DR MetOSite; Q9SXS7; -.
DR PaxDb; Q9SXS7; -.
DR PRIDE; Q9SXS7; -.
DR ProteomicsDB; 224697; -. [Q9SXS7-1]
DR EnsemblPlants; AT5G28020.1; AT5G28020.1; AT5G28020. [Q9SXS7-1]
DR EnsemblPlants; AT5G28020.2; AT5G28020.2; AT5G28020. [Q9SXS7-1]
DR EnsemblPlants; AT5G28020.3; AT5G28020.3; AT5G28020. [Q9SXS7-1]
DR EnsemblPlants; AT5G28020.4; AT5G28020.4; AT5G28020. [Q9SXS7-1]
DR EnsemblPlants; AT5G28020.6; AT5G28020.6; AT5G28020. [Q9SXS7-1]
DR GeneID; 832872; -.
DR Gramene; AT5G28020.1; AT5G28020.1; AT5G28020. [Q9SXS7-1]
DR Gramene; AT5G28020.2; AT5G28020.2; AT5G28020. [Q9SXS7-1]
DR Gramene; AT5G28020.3; AT5G28020.3; AT5G28020. [Q9SXS7-1]
DR Gramene; AT5G28020.4; AT5G28020.4; AT5G28020. [Q9SXS7-1]
DR Gramene; AT5G28020.6; AT5G28020.6; AT5G28020. [Q9SXS7-1]
DR KEGG; ath:AT5G28020; -.
DR Araport; AT5G28020; -.
DR TAIR; locus:2143814; AT5G28020.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; Q9SXS7; -.
DR OMA; YAKLEWY; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; Q9SXS7; -.
DR BioCyc; ARA:AT5G28020-MON; -.
DR SABIO-RK; Q9SXS7; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:Q9SXS7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SXS7; baseline and differential.
DR Genevisible; Q9SXS7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IMP:TAIR.
DR GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; IBA:GO_Central.
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 Alternative splicing; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Cytoplasm; Lyase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..323
FT /note="Bifunctional L-3-cyanoalanine synthase/cysteine
FT synthase D2"
FT /id="PRO_0000424459"
FT BINDING 79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 11..15
FT /note="ITELI -> VTELV (in Ref. 6; AAM62728)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="V -> I (in Ref. 5; BAH20170)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="D -> E (in Ref. 6; AAM62728)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="E -> D (in Ref. 6; AAM62728)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="Q -> R (in Ref. 7; CAB55622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 34318 MW; 877C8677BEA777F4 CRC64;
MEDRCLIKND ITELIGNTPM VYLNNVVDGC VARIAAKLEM MEPCSSVKDR IAYSMIKDAE
DKGLITPGKS TLIEPTAGNT GIGLACMGAA RGYKVILVMP STMSLERRII LRALGAELHL
SDQRIGLKGM LEKTEAILSK TPGGYIPQQF ENPANPEIHY RTTGPEIWRD SAGKVDILVA
GVGTGGTATG VGKFLKEQNK DIKVCVVEPV ESPVLSGGQP GPHLIQGIGS GIVPFNLDLT
IVDEIIQVAG EEAIETAKLL ALKEGLLVGI SSGAAAAAAL KVAKRPENAG KLIVVVFPSG
GERYLSTKLF DSIRYEAENL PIE
