ID   CYSK2_ARATH             Reviewed;         188 AA.
AC   Q9LJA0; B2GVN3;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative inactive cysteine synthase 2;
DE   AltName: Full=Beta-substituted Ala synthase 1;2;
DE            Short=ARAth-Bsas1;2;
DE   AltName: Full=O-acetylserine (thiol)-lyase 4;
GN   Name=OASA2; Synonyms=OAS4; OrderedLocusNames=At3g22460; ORFNames=F16J14.2;
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 [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10940562; DOI=10.1016/s0378-1119(00)00261-4;
RA   Jost R., Berkowitz O., Wirtz M., Hopkins L., Hawkesford M.J., Hell R.;
RT   "Genomic and functional characterization of the oas gene family encoding O-
RT   acetylserine (thiol) lyases, enzymes catalyzing the final step in cysteine
RT   biosynthesis in Arabidopsis thaliana.";
RL   Gene 253:237-247(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
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   [7]
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   [8]
RP   GENE FAMILY.
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).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. A stop codon at position
CC       188 results in a truncated and certainly non functional protein.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01461.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ272028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000731; BAB01461.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; ANM63967.1; -; Genomic_DNA.
DR   EMBL; AY063827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BT031364; ACB88823.1; -; mRNA.
DR   RefSeq; NP_001326025.1; NM_001338588.1.
DR   AlphaFoldDB; Q9LJA0; -.
DR   SMR; Q9LJA0; -.
DR   BioGRID; 7149; 11.
DR   STRING; 3702.AT3G22460.1; -.
DR   PaxDb; Q9LJA0; -.
DR   PRIDE; Q9LJA0; -.
DR   ProMEX; Q9LJA0; -.
DR   EnsemblPlants; AT3G22460.2; AT3G22460.2; AT3G22460.
DR   GeneID; 821817; -.
DR   Gramene; AT3G22460.2; AT3G22460.2; AT3G22460.
DR   KEGG; ath:AT3G22460; -.
DR   Araport; AT3G22460; -.
DR   TAIR; locus:2077041; AT3G22460.
DR   eggNOG; KOG1252; Eukaryota.
DR   HOGENOM; CLU_021018_1_1_1; -.
DR   InParanoid; Q9LJA0; -.
DR   OrthoDB; 1016546at2759; -.
DR   PhylomeDB; Q9LJA0; -.
DR   BioCyc; ARA:AT3G22460-MON; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LJA0; baseline and differential.
DR   Genevisible; Q9LJA0; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:0010043; P:response to zinc ion; IEP:TAIR.
DR   Gene3D; 3.40.50.1100; -; 2.
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   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   5: Uncertain;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..188
FT                   /note="Putative inactive cysteine synthase 2"
FT                   /id="PRO_0000424457"
FT   BINDING         80
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         184..188
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   188 AA;  19638 MW;  865DD74DDA4DE596 CRC64;
     MASVAPKIAK DVTELIGNTP LVYLNKVAKD CVGHVAAKLE MMEPCSSVKD RIGYSMIADA
     EAKGLIKPGE SVLIEPTSGN TGVGLAFTAA AKGYKLVITM PASMSIERRI ILLAFGAELI
     LTDPAKGMKG AVAKAEEILA KTPNGYMLQQ FENPANPKIH YETTGPEIWK GSGGKVDGFV
     SGIGTGGT