CYSC1_ARATH
ID CYSC1_ARATH Reviewed; 368 AA.
AC Q9S757; F4JEA0; F4JEA1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Bifunctional L-3-cyanoalanine synthase/cysteine synthase C1, mitochondrial;
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 3;1;
DE Short=ARAth-Bsas3;1;
DE AltName: Full=Cysteine synthase C1;
DE Short=AtCYSC1;
DE AltName: Full=O-acetylserine (thiol)-lyase 5;
DE Flags: Precursor;
GN Name=CYSC1; Synonyms=OAS5; OrderedLocusNames=At3g61440; ORFNames=F2A19.40;
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] (ISOFORM 1), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
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, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [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 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, FUNCTION, TISSUE SPECIFICITY, 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20935247; DOI=10.1105/tpc.110.076828;
RA Garcia I., Castellano J.M., Vioque B., Solano R., Gotor C., Romero L.C.;
RT "Mitochondrial beta-cyanoalanine synthase is essential for root hair
RT formation in Arabidopsis thaliana.";
RL Plant Cell 22:3268-3279(2010).
CC -!- FUNCTION: Acts as a major beta-cyanoalanine synthase. The cyanoalanine
CC synthesis reaction is more efficient than the cysteine synthase
CC activity. Probably unable to interact with SAT and to form the
CC decameric Cys synthase complex (CSC) and is therefore not an
CC enzymatically true OASTL protein. Probably involved in the
CC detoxification of cyanide that arises from ethylene biosynthesis.
CC Maintains a low level of cyanide for proper root hair development.
CC {ECO:0000269|PubMed:10889265, ECO:0000269|PubMed:18024555,
CC ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:20935247}.
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=39.88 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=8.03 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=8.24 mM for Na(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=0.04 mM for Na(2)S for the cysteine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=2.54 mM for L-cysteine for the L-3-cyanoalanine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=0.14 mM for L-cysteine for the L-3-cyanoalanine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=0.06 mM for KCN for the L-3-cyanoalanine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC KM=0.02 mM for KCN for the L-3-cyanoalanine synthase activity
CC {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC Vmax=0.4 umol/min/mg enzyme for L-cysteine for the cysteine synthase
CC activity {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:10889265};
CC Vmax=62.1 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
CC synthase activity {ECO:0000269|PubMed:10845460,
CC ECO:0000269|PubMed:10889265};
CC Note=kcat is 120 min(-1) for O(3)-acetyl-L-serine for the cysteine
CC synthase activity, kcat is 90 min(-1) for Na(2)S for the cysteine
CC synthase activity, kcat is 160 min(-1) for cysteine for the L-3-
CC cyanoalanine synthase activity, kcat is 130 min(-1) for KCN for the
CC L-3-cyanoalanine synthase activity.;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10845460}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9S757-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S757-2; Sequence=VSP_044070;
CC Name=3;
CC IsoId=Q9S757-3; Sequence=VSP_044069;
CC -!- TISSUE SPECIFICITY: Mainly expressed in mature rosette leaves. Also
CC detected in roots, young rosette leaves, stems, cauline leaves, and
CC flowers. {ECO:0000269|PubMed:10845460, ECO:0000269|PubMed:18024555}.
CC -!- DISRUPTION PHENOTYPE: Defective in root hair formation and accumulates
CC cyanide in root tissues. No effects on growth.
CC {ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:20935247}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AB024282; BAA78560.1; -; mRNA.
DR EMBL; AJ010505; CAB54830.1; -; mRNA.
DR EMBL; AL132962; CAB71074.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80203.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80204.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80205.1; -; Genomic_DNA.
DR EMBL; AY093094; AAM13093.1; -; mRNA.
DR EMBL; AY128782; AAM91182.1; -; mRNA.
DR EMBL; AK226606; BAE98719.1; -; mRNA.
DR EMBL; AY087208; AAM64764.1; -; mRNA.
DR PIR; T47936; T47936.
DR RefSeq; NP_001078324.1; NM_001084855.2. [Q9S757-2]
DR RefSeq; NP_001190152.1; NM_001203223.1. [Q9S757-3]
DR RefSeq; NP_191703.1; NM_116009.4. [Q9S757-1]
DR AlphaFoldDB; Q9S757; -.
DR SMR; Q9S757; -.
DR BioGRID; 10631; 1.
DR IntAct; Q9S757; 1.
DR STRING; 3702.AT3G61440.1; -.
DR iPTMnet; Q9S757; -.
DR MetOSite; Q9S757; -.
DR PaxDb; Q9S757; -.
DR PRIDE; Q9S757; -.
DR ProteomicsDB; 222750; -. [Q9S757-1]
DR EnsemblPlants; AT3G61440.1; AT3G61440.1; AT3G61440. [Q9S757-1]
DR EnsemblPlants; AT3G61440.2; AT3G61440.2; AT3G61440. [Q9S757-2]
DR EnsemblPlants; AT3G61440.3; AT3G61440.3; AT3G61440. [Q9S757-3]
DR GeneID; 825317; -.
DR Gramene; AT3G61440.1; AT3G61440.1; AT3G61440. [Q9S757-1]
DR Gramene; AT3G61440.2; AT3G61440.2; AT3G61440. [Q9S757-2]
DR Gramene; AT3G61440.3; AT3G61440.3; AT3G61440. [Q9S757-3]
DR KEGG; ath:AT3G61440; -.
DR Araport; AT3G61440; -.
DR TAIR; locus:2082837; AT3G61440.
DR eggNOG; KOG1252; Eukaryota.
DR InParanoid; Q9S757; -.
DR OMA; CILVMPE; -.
DR PhylomeDB; Q9S757; -.
DR BioCyc; ARA:AT3G61440-MON; -.
DR BRENDA; 4.4.1.9; 399.
DR SABIO-RK; Q9S757; -.
DR PRO; PR:Q9S757; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S757; baseline and differential.
DR Genevisible; Q9S757; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
DR GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IDA:TAIR.
DR GO; GO:0019500; P:cyanide catabolic process; IMP:TAIR.
DR GO; GO:0019499; P:cyanide metabolic process; TAS:TAIR.
DR GO; GO:0019344; P:cysteine biosynthetic process; IDA:TAIR.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0051410; P:detoxification of nitrogen compound; TAS:TAIR.
DR GO; GO:0006955; P:immune response; IMP:TAIR.
DR GO; GO:0080147; P:root hair cell development; IMP:TAIR.
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 Lyase; Mitochondrion; Pyridoxal phosphate; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..368
FT /note="Bifunctional L-3-cyanoalanine synthase/cysteine
FT synthase C1, mitochondrial"
FT /id="PRO_0000418635"
FT BINDING 121
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 225..229
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044069"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044070"
SQ SEQUENCE 368 AA; 39927 MW; CFDE474F4E404184 CRC64;
MASVSRRLLR RETIPCFSHT VRKLFSTVGS PSFAQRLRDL PKDFPSTNAK RDASLLIGKT
PLVFLNKVTE GCEAYVAAKQ EHFQPTCSIK DRPAIAMIAD AEKKKLIIPG KTTLIEPTSG
NMGISLAFMA AMKGYRIIMT MPSYTSLERR VTMRSFGAEL VLTDPAKGMG GTVKKAYDLL
DSTPDAFMCQ QFANPANTQI HFDTTGPEIW EDTLGNVDIF VMGIGSGGTV SGVGRYLKSK
NPNVKIYGVE PAESNILNGG KPGPHAITGN GVGFKPEILD MDVMESVLEV SSEDAIKMAR
ELALKEGLMV GISSGANTVA AIRLAKMPEN KGKLIVTIHA SFGERYLSSV LFDELRKEAE
EMKPVSVD
