ID   CAS2_MALDO              Reviewed;         375 AA.
AC   Q1KLZ1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=L-3-cyanoalanine synthase 2, mitochondrial;
DE            Short=MdCAS2;
DE            EC=4.4.1.9;
DE   Flags: Precursor;
GN   Name=CAS2;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY ETHYLENE AND WOUNDING.
RC   STRAIN=cv. Fuji;
RX   PubMed=17333023; DOI=10.1007/s00299-007-0316-9;
RA   Han S.E., Seo Y.S., Kim D., Sung S.K., Kim W.T.;
RT   "Expression of MdCAS1 and MdCAS2, encoding apple beta-cyanoalanine synthase
RT   homologs, is concomitantly induced during ripening and implicates MdCASs in
RT   the possible role of the cyanide detoxification in Fuji apple (Malus
RT   domestica Borkh.) fruits.";
RL   Plant Cell Rep. 26:1321-1331(2007).
CC   -!- FUNCTION: Probably involved in the detoxification of cyanide that
CC       arises from ethylene biosynthesis in ripening fruits. Has only
CC       background level of in vitro cysteine synthase activity.
CC       {ECO:0000269|PubMed:17333023}.
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:17333023};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, flowers and fruits.
CC       {ECO:0000269|PubMed:17333023}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during the ripening process of
CC       fruits. {ECO:0000269|PubMed:17333023}.
CC   -!- INDUCTION: Up-regulated by ethylene treatment and wounding.
CC       {ECO:0000269|PubMed:17333023}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
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DR   EMBL; DQ471309; ABF13210.1; -; mRNA.
DR   RefSeq; NP_001280751.1; NM_001293822.1.
DR   AlphaFoldDB; Q1KLZ1; -.
DR   SMR; Q1KLZ1; -.
DR   STRING; 3750.XP_008342542.1; -.
DR   GeneID; 103405317; -.
DR   KEGG; mdm:103405317; -.
DR   OrthoDB; 1016546at2759; -.
DR   BioCyc; MetaCyc:MON-16251; -.
DR   BRENDA; 4.4.1.9; 3164.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:InterPro.
DR   GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IDA:UniProtKB.
DR   GO; GO:0019499; P:cyanide metabolic process; IEA:InterPro.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0009836; P:fruit ripening, climacteric; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR031111; CAS.
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   PANTHER; PTHR10314:SF80; PTHR10314:SF80; 1.
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; Transferase; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..375
FT                   /note="L-3-cyanoalanine synthase 2, mitochondrial"
FT                   /id="PRO_0000418640"
FT   BINDING         128
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..236
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         97
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40486 MW;  DD7310016524D4D0 CRC64;
     MAALRSFLKK RSSVLCNGGA VRHRLFSAQV SQPIPDSPSF AQRIGNLPKD LPATQIKTQV
     SQLIGRTPIV YLNKVTEGCG AFIAVKQEMF QPTASIKDRP ALSMINDAEE KGLITPGETT
     LIEPTSGNMG ISMAFMAAMK GYKMVLTMPS YTSLERRVCM RCFGADLILT DPTKGMGGTV
     KKAYDLLEST PNAFMLQQFS NPANTKVHFE TTGPEIWEDT NGQVDIFVMG IGSGGTVSGV
     GQYLKSKNPN VQIYGVEPAE SNVLNGGKPG PHSITGNGVG FKPDILDMDM MERVIEVRSE
     DAVNMARQLA LKEGLMVGIS SGANTVAAME LAKKPENKGK LIVTVHASFG ERYLSSVLFQ
     DLRQEAENMQ PVAVD