ID   D7UCD0_VITVI            Unreviewed;       371 AA.
AC   D7UCD0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE            EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN   OrderedLocusNames=VIT_15s0046g02300 {ECO:0000313|EMBL:CBI40395.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI40395.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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:0000256|ARBA:ARBA00001530};
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:0000256|RuleBase:RU003985};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR605856-50, ECO:0000256|RuleBase:RU003985};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC       ECO:0000256|RuleBase:RU003985}.
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DR   EMBL; FN596755; CBI40395.3; -; Genomic_DNA.
DR   RefSeq; XP_002276013.1; XM_002275977.4.
DR   AlphaFoldDB; D7UCD0; -.
DR   STRING; 29760.D7UCD0; -.
DR   PaxDb; 29760-VIT_15s0046g02300-t01; -.
DR   EnsemblPlants; Vitvi15g01101_t001; Vitvi15g01101_P001; Vitvi15g01101.
DR   GeneID; 100255091; -.
DR   Gramene; Vitvi15g01101_t001; Vitvi15g01101_P001; Vitvi15g01101.
DR   KEGG; vvi:100255091; -.
DR   eggNOG; KOG1252; Eukaryota.
DR   HOGENOM; CLU_021018_1_0_1; -.
DR   InParanoid; D7UCD0; -.
DR   OMA; CMTADTG; -.
DR   OrthoDB; 5487987at2759; -.
DR   Proteomes; UP000009183; Chromosome 15.
DR   ExpressionAtlas; D7UCD0; baseline and differential.
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:RHEA.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003985};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW   ECO:0000256|RuleBase:RU003985};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW   ECO:0000256|RuleBase:RU003985};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          56..343
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         124
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         228..232
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   BINDING         316
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT   MOD_RES         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ   SEQUENCE   371 AA;  40499 MW;  A6720F026D431916 CRC64;
     MAALSSFFKR KSSIPFTSLA IRRWFSTQPI LDSPSFSQRI RDLPKDLPGT NIKKEVSQLI
     GKTPLVFLNK VTEGCGAYVA VKQEMMQPTA SIKDRPALAM ITDAEDKQLI TPGKTVLIEP
     TSGNMGISMA FMAAMKGYKM VLTMPSYTSL ERRVTMRAFG ADLILTDPTK GMGGTVKKAY
     ELLESTPDAF MLQQFSNPAN TQVHFETTGP EIWEDTRGQV DIFIMGIGSG GTVSGVGRYL
     KSQNPNVKIY GLEPTESNVL NGGKPGPHHI TGNGVGFKPD ILDMDVMEEV LMVSSEDAVN
     MARQLALKEG LMVGISSGAN TVAALRLARR PENKGKLIVT IHPSFGERYL SSVLFQELRK
     EAENMQPVSV D
//