CAS2_SOLTU
ID CAS2_SOLTU Reviewed; 347 AA.
AC Q9FS29;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Bifunctional L-3-cyanoalanine synthase/cysteine synthase 2, mitochondrial;
DE EC=2.5.1.47;
DE EC=4.4.1.9;
DE Flags: Precursor;
GN Name=PCAS-2;
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-157, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION BY
RP ETHYLENE AND WOUNDING.
RC STRAIN=cv. Dansyaku;
RX PubMed=11575729; DOI=10.1023/a:1011629703784;
RA Maruyama A., Saito K., Ishizawa K.;
RT "Beta-cyanoalanine synthase and cysteine synthase from potato: molecular
RT cloning, biochemical characterization, and spatial and hormonal
RT regulation.";
RL Plant Mol. Biol. 46:749-760(2001).
CC -!- FUNCTION: Has very low cyanoalanine synthase and cysteine synthase
CC activities.
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:11575729};
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;
CC Evidence={ECO:0000269|PubMed:11575729};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.14 mM for O(3)-acetyl-L-serine for the cysteine synthase
CC activity (in the presence of 2.5 mM Na(2)S)
CC {ECO:0000269|PubMed:11575729};
CC KM=1.52 mM for Na(2)S for the cysteine synthase activity (in the
CC presence of 10 mM O(3)-acetyl-L-serine)
CC {ECO:0000269|PubMed:11575729};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in tubers, buds and leaves.
CC {ECO:0000269|PubMed:11575729}.
CC -!- INDUCTION: Slightly down-regulated by ethylene treatment. No effect
CC from wounding. {ECO:0000269|PubMed:11575729}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AB029338; BAB20032.1; -; mRNA.
DR RefSeq; NP_001275044.1; NM_001288115.1.
DR AlphaFoldDB; Q9FS29; -.
DR SMR; Q9FS29; -.
DR STRING; 4113.PGSC0003DMT400000156; -.
DR ProMEX; Q9FS29; -.
DR GeneID; 102601315; -.
DR KEGG; sot:102601315; -.
DR eggNOG; KOG1252; Eukaryota.
DR InParanoid; Q9FS29; -.
DR OrthoDB; 1016546at2759; -.
DR BRENDA; 4.4.1.9; 5757.
DR SABIO-RK; Q9FS29; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q9FS29; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
DR GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IEA:UniProtKB-EC.
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 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; Lyase; Mitochondrion;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..347
FT /note="Bifunctional L-3-cyanoalanine synthase/cysteine
FT synthase 2, mitochondrial"
FT /id="PRO_0000418638"
FT BINDING 100
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 204..208
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 157
FT /note="E->N,Q: No effect on catalytic activities."
FT /evidence="ECO:0000269|PubMed:11575729"
SQ SEQUENCE 347 AA; 37636 MW; 6B85525891C0BB74 CRC64;
MATLSRFLKK RSLASNRLFS TQLPHTNIKS EVSQLIGKTP MVYLKKVTEG CGAYIAVKQE
MFQPTSSIKD RPALAMINDA EKKGLISPEK TTLIEPTSGN MGISMAFMAA MKGYKMVLTM
PSYTSMERRV TMRAFGADLI LTDPTKGMGG TVKKAYELLE STPNAFMLQQ FSNPANTQVH
FDTTGPEIWE ETLGNVDIFV MGIGSGGTVT GVGLYLKSKN PNVKIYGLEP TESNILNGGK
PGPHHITGNG VGSKPDIVDM DLMEEVLMVS SEDAVNMARE LAVKEGLMVG ISSGANTVAA
LRLAQKPENK GKLIVTVHAS FGERYLSSVL YQDLRKEAEN MQPVSVD
