CGL_ARATH
ID CGL_ARATH Reviewed; 323 AA.
AC F4K5T2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Bifunctional cystathionine gamma-lyase/cysteine synthase;
DE EC=2.5.1.47 {ECO:0000269|PubMed:19955263};
DE EC=4.4.1.1 {ECO:0000269|PubMed:19955263};
DE AltName: Full=Beta-substituted Ala synthase 4;3;
DE Short=ARAth-Bsas4;3;
DE AltName: Full=L-cysteine desulfhydrase 1;
DE Short=DES1;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OASTL;
DE AltName: Full=Protein CS-LIKE;
GN Name=DES1; OrderedLocusNames=At5g28030; ORFNames=F15F15.100;
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 [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 [2]
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 [3]
RP NOMENCLATURE.
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19955263; DOI=10.1104/pp.109.147975;
RA Alvarez C., Calo L., Romero L.C., Garcia I., Gotor C.;
RT "An O-acetylserine(thiol)lyase homolog with L-cysteine desulfhydrase
RT activity regulates cysteine homeostasis in Arabidopsis.";
RL Plant Physiol. 152:656-669(2010).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=21988475; DOI=10.1111/j.1469-8137.2011.03889.x;
RA Alvarez C., Bermudez M.A., Romero L.C., Gotor C., Garcia I.;
RT "Cysteine homeostasis plays an essential role in plant immunity.";
RL New Phytol. 193:165-177(2012).
RN [9]
RP FUNCTION.
RX PubMed=23428891; DOI=10.4161/psb.24007;
RA Romero L.C., Garcia I., Gotor C.;
RT "L-Cysteine Desulfhydrase 1 modulates the generation of the signaling
RT molecule sulfide in plant cytosol.";
RL Plant Signal. Behav. 8:0-0(2013).
CC -!- FUNCTION: Involved in maintaining Cys homeostasis through the
CC desulfuration of L-cysteine. Modulates the generation of the signaling
CC molecule sulfide in plant cytosol. Probably unable to interact with SAT
CC and to form the decameric Cys synthase complex (CSC) and is therefore
CC not an enzymatically true OASTL protein. {ECO:0000269|PubMed:18223034,
CC ECO:0000269|PubMed:19955263, ECO:0000269|PubMed:23428891}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine +
CC NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1;
CC Evidence={ECO:0000269|PubMed:19955263};
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:19955263};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:19955263};
CC -!- ACTIVITY REGULATION: Inhibited by aminooxyacetate.
CC {ECO:0000269|PubMed:19955263}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for L-cysteine for the cystathionine gamma-lyase activity
CC {ECO:0000269|PubMed:19955263};
CC KM=5.2 mM for O(3)-acetyl-L-serine for the cysteine synthase activity
CC {ECO:0000269|PubMed:19955263};
CC Vmax=0.04 umol/min/mg enzyme for the DES reaction
CC {ECO:0000269|PubMed:19955263};
CC Vmax=1.8 umol/min/mg enzyme for the OASTL reaction
CC {ECO:0000269|PubMed:19955263};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Light early-flowering and
CC premature leaf senescence phenotype. Increased total cysteine content
CC and increased resistance to pathogens. {ECO:0000269|PubMed:18024555,
CC ECO:0000269|PubMed:19955263, ECO:0000269|PubMed:21988475}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AC007627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93765.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93766.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68869.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68870.1; -; Genomic_DNA.
DR RefSeq; NP_001330587.1; NM_001344055.1.
DR RefSeq; NP_001330588.1; NM_001344054.1.
DR RefSeq; NP_198155.1; NM_122686.2.
DR RefSeq; NP_974843.1; NM_203114.2.
DR AlphaFoldDB; F4K5T2; -.
DR SMR; F4K5T2; -.
DR STRING; 3702.AT5G28030.1; -.
DR PaxDb; F4K5T2; -.
DR PRIDE; F4K5T2; -.
DR ProteomicsDB; 222075; -.
DR EnsemblPlants; AT5G28030.1; AT5G28030.1; AT5G28030.
DR EnsemblPlants; AT5G28030.2; AT5G28030.2; AT5G28030.
DR EnsemblPlants; AT5G28030.4; AT5G28030.4; AT5G28030.
DR EnsemblPlants; AT5G28030.5; AT5G28030.5; AT5G28030.
DR GeneID; 832873; -.
DR Gramene; AT5G28030.1; AT5G28030.1; AT5G28030.
DR Gramene; AT5G28030.2; AT5G28030.2; AT5G28030.
DR Gramene; AT5G28030.4; AT5G28030.4; AT5G28030.
DR Gramene; AT5G28030.5; AT5G28030.5; AT5G28030.
DR KEGG; ath:AT5G28030; -.
DR Araport; AT5G28030; -.
DR TAIR; locus:2143754; AT5G28030.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; F4K5T2; -.
DR OMA; KQPEYAG; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; F4K5T2; -.
DR BRENDA; 4.4.1.28; 399.
DR SABIO-RK; F4K5T2; -.
DR UniPathway; UPA00136; UER00200.
DR PRO; PR:F4K5T2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K5T2; baseline and differential.
DR Genevisible; F4K5T2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004123; F:cystathionine gamma-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:UniProtKB.
DR GO; GO:0080146; F:L-cysteine desulfhydrase activity; IDA:UniProtKB.
DR GO; GO:0044540; F:L-cystine L-cysteine-lyase (deaminating); IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
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 GO; GO:0080145; P:cysteine homeostasis; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:1990170; P:stress response to cadmium ion; 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 Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..323
FT /note="Bifunctional cystathionine gamma-lyase/cysteine
FT synthase"
FT /id="PRO_0000418598"
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"
SQ SEQUENCE 323 AA; 34326 MW; 5F8E4924D7CDED9F CRC64;
MEDRVLIKND VTELIGNTPM VYLNKIVDGC VARIAAKLEM MEPCSSIKDR IAYSMIKDAE
DKGLITPGKS TLIEATGGNT GIGLASIGAS RGYKVILLMP STMSLERRII LRALGAEVHL
TDISIGIKGQ LEKAKEILSK TPGGYIPHQF INPENPEIHY RTTGPEIWRD SAGKVDILVA
GVGTGGTVTG TGKFLKEKNK DIKVCVVEPS ESAVLSGGKP GPHLIQGIGS GEIPANLDLS
IVDEIIQVTG EEAIETTKLL AIKEGLLVGI SSGASAAAAL KVAKRPENVG KLIVVIFPSG
GERYLSTELF ESVRYEAENL PVE
