CYSK4_ARATH
ID CYSK4_ARATH Reviewed; 404 AA.
AC O22682;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent), chloroplastic {ECO:0000305};
DE EC=2.5.1.144 {ECO:0000269|PubMed:20179139};
DE AltName: Full=AtCS26 {ECO:0000303|PubMed:18223034};
DE AltName: Full=Beta-substituted Ala synthase 5;1 {ECO:0000303|PubMed:18024555};
DE Short=ARAth-Bsas5;1 {ECO:0000303|PubMed:18024555};
DE AltName: Full=O-acetylserine sulfhydrylase {ECO:0000305};
DE Flags: Precursor;
GN Name=CS26 {ECO:0000303|PubMed:18223034};
GN OrderedLocusNames=At3g03630 {ECO:0000312|Araport:AT3G03630};
GN ORFNames=T12J13.9 {ECO:0000312|EMBL:AAF03469.1};
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].
RC STRAIN=cv. Columbia;
RA Nakamura T., Koizumi N., Sano H.;
RT "Isolation of a novel cysteine synthase cDNA from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-081(1997).
RN [2]
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 [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 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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [8]
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 [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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20179139; DOI=10.1105/tpc.109.071985;
RA Bermudez M.A., Paez-Ochoa M.A., Gotor C., Romero L.C.;
RT "Arabidopsis S-sulfocysteine synthase activity is essential for chloroplast
RT function and long-day light-dependent redox control.";
RL Plant Cell 22:403-416(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22829322; DOI=10.1104/pp.112.201491;
RA Bermudez M.A., Galmes J., Moreno I., Mullineaux P.M., Gotor C.,
RA Romero L.C.;
RT "Photosynthetic adaptation to length of day is dependent on S-sulfocysteine
RT synthase activity in the thylakoid lumen.";
RL Plant Physiol. 160:274-288(2012).
RN [12]
RP FUNCTION.
RX PubMed=23333972; DOI=10.4161/psb.23313;
RA Gotor C., Romero L.C.;
RT "S-sulfocysteine synthase function in sensing chloroplast redox status.";
RL Plant Signal. Behav. 8:0-0(2013).
CC -!- FUNCTION: S-sulfocysteine synthase that plays an important role in
CC chloroplast function and is essential for light-dependent redox
CC regulation and photosynthetic performance within the chloroplast
CC (PubMed:20179139, PubMed:22829322, PubMed:23333972). Probably unable to
CC interact with SAT and to form the decameric Cys synthase complex (CSC)
CC required for O-acetylserine (thiol)-lyase (OAS-TL) enzymatic activity
CC (PubMed:18223034). Lacks OAS-TL activity (PubMed:20179139).
CC {ECO:0000269|PubMed:18223034, ECO:0000269|PubMed:20179139,
CC ECO:0000269|PubMed:22829322, ECO:0000269|PubMed:23333972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O-acetyl-L-serine + thiosulfate = acetate + H(+) + S-sulfo-L-
CC cysteine; Xref=Rhea:RHEA:30891, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:33542, ChEBI:CHEBI:58340, ChEBI:CHEBI:62225;
CC EC=2.5.1.144; Evidence={ECO:0000269|PubMed:20179139};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P0A1E3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.46 mM for O-acetyl-L-serine {ECO:0000269|PubMed:20179139};
CC KM=0.93 mM for thiosulfate {ECO:0000269|PubMed:20179139};
CC Vmax=20.7 mmol/min/mg enzyme toward thiosulfate
CC {ECO:0000269|PubMed:20179139};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:20179139};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:20179139};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:22829322}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition (PubMed:18024555). No visible phenotype under short day (SD)
CC conditions (PubMed:20179139). Reduced growth and pale green leaf
CC phenotype under long day (LD) conditions (PubMed:20179139,
CC PubMed:22829322). {ECO:0000269|PubMed:18024555,
CC ECO:0000269|PubMed:20179139, ECO:0000269|PubMed:22829322}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB003041; BAA21628.1; -; mRNA.
DR EMBL; AC009327; AAF03469.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73965.1; -; Genomic_DNA.
DR EMBL; AY099573; AAM20425.1; -; mRNA.
DR EMBL; BT002155; AAN72166.1; -; mRNA.
DR RefSeq; NP_187013.1; NM_111234.5.
DR AlphaFoldDB; O22682; -.
DR SMR; O22682; -.
DR BioGRID; 6536; 1.
DR IntAct; O22682; 1.
DR STRING; 3702.AT3G03630.1; -.
DR PaxDb; O22682; -.
DR PRIDE; O22682; -.
DR ProteomicsDB; 224041; -.
DR EnsemblPlants; AT3G03630.1; AT3G03630.1; AT3G03630.
DR GeneID; 821203; -.
DR Gramene; AT3G03630.1; AT3G03630.1; AT3G03630.
DR KEGG; ath:AT3G03630; -.
DR Araport; AT3G03630; -.
DR TAIR; locus:2096454; AT3G03630.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_1_1; -.
DR InParanoid; O22682; -.
DR OMA; EDAYEMS; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; O22682; -.
DR BioCyc; ARA:AT3G03630-MON; -.
DR BioCyc; MetaCyc:AT3G03630-MON; -.
DR BRENDA; 2.5.1.47; 399.
DR PRO; PR:O22682; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; O22682; baseline and differential.
DR Genevisible; O22682; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031977; C:thylakoid lumen; IDA:TAIR.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
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:0015979; P:photosynthesis; IMP:TAIR.
DR GO; GO:0009643; P:photosynthetic acclimation; IMP:TAIR.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:TAIR.
DR GO; GO:0090322; P:regulation of superoxide metabolic process; 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; Chloroplast; Cysteine biosynthesis; Plastid;
KW Pyridoxal phosphate; Reference proteome; Thylakoid; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..84
FT /note="Thylakoid"
FT /evidence="ECO:0000255"
FT CHAIN 85..404
FT /note="S-sulfo-L-cysteine synthase (O-acetyl-L-serine-
FT dependent), chloroplastic"
FT /id="PRO_0000006354"
FT REGION 61..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT BINDING 275..279
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT BINDING 353
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
FT MOD_RES 140
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A1E3"
SQ SEQUENCE 404 AA; 43161 MW; 50C813C470B1CF64 CRC64;
MAFASPSLRL LPQSPLGRIT SKLHRFSTAK LSLFSFHHDS SSSLAVRTPV SSFVVGAISG
KSSTGTKSKS KTKRKPPPPP PVTTVAEEQH IAESETVNIA EDVTQLIGST PMVYLNRVTD
GCLADIAAKL ESMEPCRSVK DRIGLSMINE AENSGAITPR KTVLVEPTTG NTGLGIAFVA
AAKGYKLIVT MPASINIERR MLLRALGAEI VLTNPEKGLK GAVDKAKEIV LKTKNAYMFQ
QFDNTANTKI HFETTGPEIW EDTMGNVDIF VAGIGTGGTV TGTGGFLKMM NKDIKVVGVE
PSERSVISGD NPGYLPGILD VKLLDEVFKV SNGEAIEMAR RLALEEGLLV GISSGAAAVA
AVSLAKRAEN AGKLITVLFP SHGERYITTA LFSSINREVQ EMRY
