CYSK2_BRAJU
ID CYSK2_BRAJU Reviewed; 324 AA.
AC O23735;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cysteine synthase;
DE Short=CSase;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine (thiol)-lyase;
DE Short=OAS-TL;
DE AltName: Full=O-acetylserine sulfhydrylase;
DE AltName: Full=OAS-TL6;
OS Brassica juncea (Indian mustard) (Sinapis juncea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3707;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Vittasso; TISSUE=Root;
RX PubMed=9620267; DOI=10.1023/a:1005929022061;
RA Schaefer H.J., Haag-Kerwer A., Rausch T.H.;
RT "cDNA cloning and expression analysis of genes encoding GSH synthesis in
RT roots of the heavy-metal accumulator Brassica juncea L.: evidence for Cd-
RT induction of a putative mitochondrial gamma-glutamylcysteine synthetase
RT isoform.";
RL Plant Mol. Biol. 37:87-97(1998).
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; Y10847; CAA71800.1; -; mRNA.
DR AlphaFoldDB; O23735; -.
DR SMR; O23735; -.
DR PRIDE; O23735; -.
DR UniPathway; UPA00136; UER00200.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..324
FT /note="Cysteine synthase"
FT /id="PRO_0000167118"
FT BINDING 79
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 183..187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 324 AA; 34132 MW; 091B5B2C0BED1EA1 CRC64;
MASRIGIAND VTELIGNTPL VYLNSVAEGC VGRVAAKLEM MEPCSSVKDR IGFSMISDAE
KKGLIKPGES VLIEPTSGNT GVGLAFTAAA KGYKLIITMP ASMSIERRII LLAFGVELVL
TDPAKGMKGA IAKAEEILAK TPNGYMLQQF ENPANPKIHY ETTGPEIWKG TEGKIDGFIS
GIGTGGTITG AGKYLKEQNP NVKLYGVEPV ESAILSGGKP GPHKIQGIGA GFIPNVLETN
LIDEVVQVSS DESIDMARLL AREEGLLVGI SSGAAAAAAI KLAKRPENAG KLFVAVFPSF
GERYLSTVLF DATRKEAESM TFEA
