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Cysteine synthase, chloroplastic/chromoplastic (EC 2.5.1.47) (At.OAS.7-4) (Beta-substituted Ala synthase 2;1) (ARAth-Bsas2;1) (CSase B) (AtCS-B) (CS-B) (O-acetylserine (thiol)-lyase) (O-acetylserine sulfhydrylase) (OAS-TL B) (cpACS1)

 CYSKP_ARATH             Reviewed;         392 AA.
P47999; O22828; Q42568;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 147.
RecName: Full=Cysteine synthase, chloroplastic/chromoplastic;
EC=2.5.1.47;
AltName: Full=At.OAS.7-4;
AltName: Full=Beta-substituted Ala synthase 2;1;
Short=ARAth-Bsas2;1;
AltName: Full=CSase B;
Short=AtCS-B;
Short=CS-B;
AltName: Full=O-acetylserine (thiol)-lyase;
AltName: Full=O-acetylserine sulfhydrylase;
AltName: Full=OAS-TL B;
AltName: Full=cpACS1;
Flags: Precursor;
Name=OASB; OrderedLocusNames=At2g43750; ORFNames=F18O19.14;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=8082776; DOI=10.1016/0014-5793(94)00872-8;
Hell R., Bork C., Bogdanova N., Frolov I., Hauschild R.;
"Isolation and characterization of two cDNAs encoding for compartment
specific isoforms of O-acetylserine (thiol) lyase from Arabidopsis
thaliana.";
FEBS Lett. 351:257-262(1994).
[2]
SEQUENCE REVISION [MRNA].
Hell R.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=7610184; DOI=10.1104/pp.108.2.851;
Hesse H., Altmann T.;
"Molecular cloning of a cysteine synthase cDNA from Arabidopsis
thaliana.";
Plant Physiol. 108:851-852(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=cv. Columbia;
PubMed=10940562; DOI=10.1016/S0378-1119(00)00261-4;
Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
"Genomic and functional characterization of the oas gene family
encoding O-acetylserine (thiol) lyases, enzymes catalyzing the final
step in cysteine biosynthesis in Arabidopsis thaliana.";
Gene 253:237-247(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[6]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NOMENCLATURE.
PubMed=10889265; DOI=10.1104/pp.123.3.1163;
Hatzfeld Y., Maruyama A., Schmidt A., Noji M., Ishizawa K., Saito K.;
"beta-Cyanoalanine synthase is a mitochondrial cysteine synthase-like
protein in spinach and Arabidopsis.";
Plant Physiol. 123:1163-1171(2000).
[10]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15258168; DOI=10.1093/jxb/erh201;
Wirtz M., Droux M., Hell R.;
"O-acetylserine (thiol) lyase: an enigmatic enzyme of plant cysteine
biosynthesis revisited in Arabidopsis thaliana.";
J. Exp. Bot. 55:1785-1798(2004).
[11]
REVIEW.
PubMed=16307301; DOI=10.1007/s11120-005-8810-9;
Wirtz M., Droux M.;
"Synthesis of the sulfur amino acids: cysteine and methionine.";
Photosyn. Res. 86:345-362(2005).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18223034; DOI=10.1105/tpc.107.056747;
Heeg C., Kruse C., Jost R., Gutensohn M., Ruppert T., Wirtz M.,
Hell R.;
"Analysis of the Arabidopsis O-acetylserine(thiol)lyase gene family
demonstrates compartment-specific differences in the regulation of
cysteine synthesis.";
Plant Cell 20:168-185(2008).
[13]
GENE FAMILY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18024555; DOI=10.1104/pp.107.106831;
Watanabe M., Kusano M., Oikawa A., Fukushima A., Noji M., Saito K.;
"Physiological roles of the beta-substituted alanine synthase gene
family in Arabidopsis.";
Plant Physiol. 146:310-320(2008).
[14]
ACETYLATION AT ALA-61, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20658158; DOI=10.1007/s00726-010-0694-0;
Wirtz M., Heeg C., Samami A.A., Ruppert T., Hell R.;
"Enzymes of cysteine synthesis show extensive and conserved
modifications patterns that include N(alpha)-terminal acetylation.";
Amino Acids 39:1077-1086(2010).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-61, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER LYS-60, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
-!- FUNCTION: Acts as a major cysteine synthase.
{ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034}.
-!- CATALYTIC ACTIVITY: O-acetyl-L-serine + hydrogen sulfide = L-
cysteine + acetate. {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.81 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
KM=0.31 mM for O(3)-acetyl-L-serine for the cysteine synthase
activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
KM=3.0 uM for H(2)S for the cysteine synthase activity
{ECO:0000269|PubMed:10940562, ECO:0000269|PubMed:15258168};
Vmax=171 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
Vmax=592 umol/min/mg enzyme for L-cysteine for the cysteine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
Vmax=0.37 umol/min/mg enzyme for H(2)S for the L-3-cyanoalanine
synthase activity {ECO:0000269|PubMed:10940562,
ECO:0000269|PubMed:15258168};
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-serine: step 2/2.
-!- SUBUNIT: Homodimer. Component of the cysteine synthase complex
(CSC) composed of two OAS-TL dimers and one SAT hexamer (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid,
chromoplast.
-!- DISRUPTION PHENOTYPE: No visible phenotype.
{ECO:0000269|PubMed:18024555, ECO:0000269|PubMed:18223034}.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X80377; CAA56594.2; -; mRNA.
EMBL; X81698; CAA57344.1; -; mRNA.
EMBL; AJ271728; CAB71292.1; -; Genomic_DNA.
EMBL; AC002333; AAB64031.1; -; Genomic_DNA.
EMBL; CP002685; AEC10317.1; -; Genomic_DNA.
EMBL; CP002685; AEC10318.1; -; Genomic_DNA.
EMBL; AY065375; AAL38816.1; -; mRNA.
EMBL; AY096681; AAM20315.1; -; mRNA.
EMBL; AY086156; AAM63361.1; -; mRNA.
PIR; A84870; A84870.
PIR; S48695; S48695.
RefSeq; NP_001189745.1; NM_001202816.1.
RefSeq; NP_181903.1; NM_129937.4.
UniGene; At.20491; -.
UniGene; At.72689; -.
ProteinModelPortal; P47999; -.
SMR; P47999; -.
BioGrid; 4314; 4.
IntAct; P47999; 1.
STRING; 3702.AT2G43750.1; -.
iPTMnet; P47999; -.
SWISS-2DPAGE; P47999; -.
PaxDb; P47999; -.
PRIDE; P47999; -.
EnsemblPlants; AT2G43750.1; AT2G43750.1; AT2G43750.
EnsemblPlants; AT2G43750.2; AT2G43750.2; AT2G43750.
GeneID; 818978; -.
Gramene; AT2G43750.1; AT2G43750.1; AT2G43750.
Gramene; AT2G43750.2; AT2G43750.2; AT2G43750.
KEGG; ath:AT2G43750; -.
Araport; AT2G43750; -.
TAIR; locus:2043964; AT2G43750.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
HOGENOM; HOG000217394; -.
InParanoid; P47999; -.
KO; K01738; -.
OMA; SPMQFEN; -.
OrthoDB; EOG09360FNG; -.
PhylomeDB; P47999; -.
BioCyc; MetaCyc:AT2G43750-MONOMER; -.
UniPathway; UPA00136; UER00200.
PRO; PR:P47999; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; P47999; baseline and differential.
Genevisible; P47999; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0009536; C:plastid; TAS:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0004124; F:cysteine synthase activity; IDA:TAIR.
GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0019344; P:cysteine biosynthetic process; IDA:TAIR.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IGI:TAIR.
GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009735; P:response to cytokinin; IDA:TAIR.
InterPro; IPR005856; Cys_synth.
InterPro; IPR005859; CysK.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00291; PALP; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01139; cysK; 1.
TIGRFAMs; TIGR01136; cysKM; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
1: Evidence at protein level;
Acetylation; Amino-acid biosynthesis; Chloroplast; Chromoplast;
Complete proteome; Cysteine biosynthesis; Plastid;
Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
TRANSIT 1 60 Chloroplast and chromoplast.
{ECO:0000244|PubMed:22223895}.
CHAIN 61 392 Cysteine synthase,
chloroplastic/chromoplastic.
/FTId=PRO_0000006349.
REGION 251 255 Pyridoxal phosphate binding.
{ECO:0000250}.
COMPBIAS 342 347 Poly-Ala.
BINDING 147 147 Pyridoxal phosphate. {ECO:0000250}.
BINDING 339 339 Pyridoxal phosphate. {ECO:0000250}.
MOD_RES 61 61 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000269|PubMed:20658158}.
MOD_RES 116 116 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
CONFLICT 232 232 G -> N (in Ref. 3; CAA57344).
{ECO:0000305}.
CONFLICT 288 288 P -> T (in Ref. 3; CAA57344).
{ECO:0000305}.
SEQUENCE 392 AA; 41656 MW; B1220F01E8E31A12 CRC64;
MAATSSSAFL LNPLTSRHRP FKYSPELSSL SLSSRKAAAF DVSSAAFTLK RQSRSDVVCK
AVSIKPEAGV EGLNIADNAA QLIGKTPMVY LNNVVKGCVA SVAAKLEIME PCCSVKDRIG
YSMITDAEEK GLITPGKSVL VESTSGNTGI GLAFIAASKG YKLILTMPAS MSLERRVLLR
AFGAELVLTE PAKGMTGAIQ KAEEILKKTP NSYMLQQFDN PANPKIHYET TGPEIWEDTR
GKIDILVAGI GTGGTITGVG RFIKERKPEL KVIGVEPTES AILSGGKPGP HKIQGIGAGF
VPKNLDLAIV DEYIAISSEE AIETSKQLAL QEGLLVGISS GAAAAAAIQV AKRPENAGKL
IAVVFPSFGE RYLSTQLFQS IREECEQMQP EL


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