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Protein

Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2

Gene

CYSD2

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

Functioni

Acts as a cysteine synthase. The cysteine synthesis reaction is more efficient than the cyanoalanine synthase activity.1 Publication

Catalytic activityi

O-acetyl-L-serine + hydrogen sulfide = L-cysteine + acetate.1 Publication
L-cysteine + hydrogen cyanide = L-3-cyanoalanine + hydrogen sulfide.1 Publication

Cofactori

Kineticsi

  1. KM=7.97 mM for O(3)-acetyl-L-serine for the cysteine synthase activity1 Publication
  2. KM=0.25 mM for Na2S for the cysteine synthase activity1 Publication

    Pathwayi: L-cysteine biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes L-cysteine from L-serine.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Serine acetyltransferase 3, mitochondrial (SAT3), Serine acetyltransferase 5 (SAT5), Serine acetyltransferase 1, chloroplastic (SAT1), Serine acetyltransferase 2 (SAT2), Serine acetyltransferase 4 (SAT4)
    2. Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2 (CYSD2), Bifunctional cystathionine gamma-lyase/cysteine synthase (DES1), Cysteine synthase, mitochondrial (OASC), Bifunctional L-3-cyanoalanine synthase/cysteine synthase D1 (CYSD1), Cysteine synthase, chloroplastic/chromoplastic (OASB), Cysteine synthase 1 (OASA1)
    This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791Pyridoxal phosphateBy similarity
    Binding sitei271 – 2711Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    • cysteine synthase activity Source: TAIR
    • L-3-cyanoalanine synthase activity Source: UniProtKB-EC
    • pyridoxal phosphate binding Source: GO_Central
    • transferase activity Source: UniProtKB-KW

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciARA:AT5G28020-MONOMER.
    ARA:GQT-2028-MONOMER.
    ARA:GQT-2212-MONOMER.
    ARA:GQT-985-MONOMER.
    ARA:GQT-986-MONOMER.
    ARA:GQT-987-MONOMER.
    UniPathwayiUPA00136; UER00200.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2 (EC:2.5.1.471 Publication, EC:4.4.1.91 Publication)
    Alternative name(s):
    Beta-substituted Ala synthase 4;2
    Short name:
    ARAth-Bsas4;2
    Cysteine synthase D2
    Short name:
    AtcysD2
    O-acetylserine (thiol)-lyase 6
    Gene namesi
    Name:CYSD2
    Synonyms:OAS6
    Ordered Locus Names:At5g28020
    ORF Names:F15F15.90
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G28020.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Bifunctional L-3-cyanoalanine synthase/cysteine synthase D2PRO_0000424459Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiQ9SXS7.
    PRIDEiQ9SXS7.

    Expressioni

    Tissue specificityi

    Predominantly expressed in leaves and flowers.1 Publication

    Inductioni

    By nitrogen starvation.1 Publication

    Gene expression databases

    ExpressionAtlasiQ9SXS7. baseline and differential.
    GenevisibleiQ9SXS7. AT.

    Interactioni

    Protein-protein interaction databases

    BioGridi18146. 2 interactions.
    IntActiQ9SXS7. 1 interaction.
    STRINGi3702.AT5G28020.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SXS7.
    SMRiQ9SXS7. Positions 7-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni183 – 1875Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1252. Eukaryota.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    InParanoidiQ9SXS7.
    KOiK01738.
    OMAiVIEYTSG.
    PhylomeDBiQ9SXS7.

    Family and domain databases

    InterProiIPR005856. Cys_synth.
    IPR005859. CysK.
    IPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01139. cysK. 1 hit.
    TIGR01136. cysKM. 1 hit.
    PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

    Note: A number of isoforms are produced. According to EST sequences.

    Isoform 1 (identifier: Q9SXS7-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MEDRCLIKND ITELIGNTPM VYLNNVVDGC VARIAAKLEM MEPCSSVKDR
    60 70 80 90 100
    IAYSMIKDAE DKGLITPGKS TLIEPTAGNT GIGLACMGAA RGYKVILVMP
    110 120 130 140 150
    STMSLERRII LRALGAELHL SDQRIGLKGM LEKTEAILSK TPGGYIPQQF
    160 170 180 190 200
    ENPANPEIHY RTTGPEIWRD SAGKVDILVA GVGTGGTATG VGKFLKEQNK
    210 220 230 240 250
    DIKVCVVEPV ESPVLSGGQP GPHLIQGIGS GIVPFNLDLT IVDEIIQVAG
    260 270 280 290 300
    EEAIETAKLL ALKEGLLVGI SSGAAAAAAL KVAKRPENAG KLIVVVFPSG
    310 320
    GERYLSTKLF DSIRYEAENL PIE
    Length:323
    Mass (Da):34,318
    Last modified:May 1, 2000 - v1
    Checksum:i877C8677BEA777F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 155ITELI → VTELV in AAM62728 (Ref. 6) Curated
    Sequence conflicti26 – 261V → I in BAH20170 (PubMed:19423640).Curated
    Sequence conflicti61 – 611D → E in AAM62728 (Ref. 6) Curated
    Sequence conflicti117 – 1171E → D in AAM62728 (Ref. 6) Curated
    Sequence conflicti148 – 1481Q → R in CAB55622 (PubMed:10889265).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB024283 mRNA. Translation: BAA78561.1.
    AC007627 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED93759.1.
    CP002688 Genomic DNA. Translation: AED93760.1.
    CP002688 Genomic DNA. Translation: AED93761.1.
    CP002688 Genomic DNA. Translation: AED93762.1.
    CP002688 Genomic DNA. Translation: AED93764.1.
    AF424598 mRNA. Translation: AAL11592.1.
    AY124831 mRNA. Translation: AAM70540.1.
    AK317505 mRNA. Translation: BAH20170.1.
    AY085504 mRNA. Translation: AAM62728.1.
    AJ011044 mRNA. Translation: CAB55622.1.
    PIRiT52661.
    RefSeqiNP_001031956.1. NM_001036879.1. [Q9SXS7-1]
    NP_001031957.1. NM_001036880.2. [Q9SXS7-1]
    NP_001078628.1. NM_001085159.1. [Q9SXS7-1]
    NP_198154.1. NM_122685.2. [Q9SXS7-1]
    NP_851087.1. NM_180756.2. [Q9SXS7-1]
    UniGeneiAt.23896.

    Genome annotation databases

    EnsemblPlantsiAT5G28020.1; AT5G28020.1; AT5G28020. [Q9SXS7-1]
    AT5G28020.2; AT5G28020.2; AT5G28020. [Q9SXS7-1]
    AT5G28020.3; AT5G28020.3; AT5G28020. [Q9SXS7-1]
    AT5G28020.4; AT5G28020.4; AT5G28020. [Q9SXS7-1]
    AT5G28020.6; AT5G28020.6; AT5G28020. [Q9SXS7-1]
    GeneIDi832872.
    KEGGiath:AT5G28020.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB024283 mRNA. Translation: BAA78561.1.
    AC007627 Genomic DNA. No translation available.
    CP002688 Genomic DNA. Translation: AED93759.1.
    CP002688 Genomic DNA. Translation: AED93760.1.
    CP002688 Genomic DNA. Translation: AED93761.1.
    CP002688 Genomic DNA. Translation: AED93762.1.
    CP002688 Genomic DNA. Translation: AED93764.1.
    AF424598 mRNA. Translation: AAL11592.1.
    AY124831 mRNA. Translation: AAM70540.1.
    AK317505 mRNA. Translation: BAH20170.1.
    AY085504 mRNA. Translation: AAM62728.1.
    AJ011044 mRNA. Translation: CAB55622.1.
    PIRiT52661.
    RefSeqiNP_001031956.1. NM_001036879.1. [Q9SXS7-1]
    NP_001031957.1. NM_001036880.2. [Q9SXS7-1]
    NP_001078628.1. NM_001085159.1. [Q9SXS7-1]
    NP_198154.1. NM_122685.2. [Q9SXS7-1]
    NP_851087.1. NM_180756.2. [Q9SXS7-1]
    UniGeneiAt.23896.

    3D structure databases

    ProteinModelPortaliQ9SXS7.
    SMRiQ9SXS7. Positions 7-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi18146. 2 interactions.
    IntActiQ9SXS7. 1 interaction.
    STRINGi3702.AT5G28020.1.

    Proteomic databases

    PaxDbiQ9SXS7.
    PRIDEiQ9SXS7.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G28020.1; AT5G28020.1; AT5G28020. [Q9SXS7-1]
    AT5G28020.2; AT5G28020.2; AT5G28020. [Q9SXS7-1]
    AT5G28020.3; AT5G28020.3; AT5G28020. [Q9SXS7-1]
    AT5G28020.4; AT5G28020.4; AT5G28020. [Q9SXS7-1]
    AT5G28020.6; AT5G28020.6; AT5G28020. [Q9SXS7-1]
    GeneIDi832872.
    KEGGiath:AT5G28020.

    Organism-specific databases

    TAIRiAT5G28020.

    Phylogenomic databases

    eggNOGiKOG1252. Eukaryota.
    COG0031. LUCA.
    HOGENOMiHOG000217394.
    InParanoidiQ9SXS7.
    KOiK01738.
    OMAiVIEYTSG.
    PhylomeDBiQ9SXS7.

    Enzyme and pathway databases

    UniPathwayiUPA00136; UER00200.
    BioCyciARA:AT5G28020-MONOMER.
    ARA:GQT-2028-MONOMER.
    ARA:GQT-2212-MONOMER.
    ARA:GQT-985-MONOMER.
    ARA:GQT-986-MONOMER.
    ARA:GQT-987-MONOMER.

    Miscellaneous databases

    PROiQ9SXS7.

    Gene expression databases

    ExpressionAtlasiQ9SXS7. baseline and differential.
    GenevisibleiQ9SXS7. AT.

    Family and domain databases

    InterProiIPR005856. Cys_synth.
    IPR005859. CysK.
    IPR001216. P-phosphate_BS.
    IPR001926. TrpB-like_PLP-dep.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01139. cysK. 1 hit.
    TIGR01136. cysKM. 1 hit.
    PROSITEiPS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Three Arabidopsis genes encoding proteins with differential activities for cysteine synthase and beta-cyanoalanine synthase."
      Yamaguchi Y., Nakamura T., Kusano T., Sano H.
      Plant Cell Physiol. 41:465-476(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY NITROGEN STARVATION, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
    2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.
    5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
      Tissue: Rosette leaf.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like protein in spinach and Arabidopsis."
      Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.
      Plant Physiol. 123:1163-1171(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 148-323, NOMENCLATURE.
      Strain: cv. Columbia.
    8. "Synthesis of the sulfur amino acids: cysteine and methionine."
      Wirtz M., Droux M.
      Photosyn. Res. 86:345-362(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    9. "Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family demonstrates compartment-specific differences in the regulation of cysteine synthesis."
      Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M., Hell R.
      Plant Cell 20:168-185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
    10. "Physiological roles of the beta-substituted alanine synthase gene family in Arabidopsis."
      Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.
      Plant Physiol. 146:310-320(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, DISRUPTION PHENOTYPE.
    11. "Enzymes of cysteine synthesis show extensive and conserved modifications patterns that include N(alpha)-terminal acetylation."
      Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.
      Amino Acids 39:1077-1086(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCYSD2_ARATH
    AccessioniPrimary (citable) accession number: Q9SXS7
    Secondary accession number(s): B9DHF3, Q8LEC3, Q9SMY4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2013
    Last sequence update: May 1, 2000
    Last modified: February 17, 2016
    This is version 112 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.