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 27-MAR-2024, entry version 73.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ471308; ABF13209.1; -; mRNA.
DR RefSeq; NP_001280949.1; NM_001294020.1.
DR AlphaFoldDB; Q1KLZ2; -.
DR SMR; Q1KLZ2; -.
DR GeneID; 103401891; -.
DR KEGG; mdm:103401891; -.
DR OrthoDB; 5487987at2759; -.
DR BioCyc; MetaCyc:MONOMER-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: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 CDD; cd01561; CBS_like; 1.
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; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01139; cysK; 1.
DR NCBIfam; TIGR01136; cysKM; 1.
DR PANTHER; PTHR10314:SF80; BIFUNCTIONAL L-3-CYANOALANINE SYNTHASE_CYSTEINE SYNTHASE C1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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
//
