ID   CAS1_MALDO              Reviewed;         376 AA.
AC   Q1KLZ2;
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 1, mitochondrial;
DE            Short=MdCAS1;
DE            EC=4.4.1.9;
DE   Flags: Precursor;
GN   Name=CAS1;
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.
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 ethylen 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; DQ471308; ABF13209.1; -; mRNA.
DR   RefSeq; NP_001280949.1; NM_001294020.1.
DR   AlphaFoldDB; Q1KLZ2; -.
DR   SMR; Q1KLZ2; -.
DR   STRING; 3750.XP_008338826.1; -.
DR   GeneID; 103401891; -.
DR   KEGG; mdm:103401891; -.
DR   OrthoDB; 1016546at2759; -.
DR   BioCyc; MetaCyc:MON-16250; -.
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   GO; GO:0009611; P:response to wounding; IDA:CACAO.
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..14
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..376
FT                   /note="L-3-cyanoalanine synthase 1, mitochondrial"
FT                   /id="PRO_0000418639"
FT   BINDING         127
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         96
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  40883 MW;  77BF8BAB1EBA914C CRC64;
     MAALRSFLKK RSSVLCNGAM RRKLFSTEVS QPLTDSPSFA QRIRNLPKDL PGTQIKTQVS
     QLIGRTPIVY LNKVTEGCGA YIAVKQEMFQ PTASIKDRPA LSMINDAEEK GLITPGETIL
     IEPTSGNMGI SMAFMAAMRG YKMVLTMPSY TSLERRVCMR CFGADLILTD PTKGMGGTVK
     KAYDLLESTP NAYMLQQFSN PANTKVHFET TGPEIWEDTN GQVDIFVMGI GSGGTVSGVG
     QYLKSKNPNV QIYGVEPAES NVLNGGKPGP HSIMGNGVGF KPDILDLDML ERVIEVTSED
     AVNMARQLAL KEGLMVGISS GANTVAAMEL AKKPENKGKL IVTVHPSFGE RYLSSVLFQE
     LRQEAENMQP VAVDYP