ID M7Z105_TRIUA Unreviewed; 339 AA.
AC M7Z105;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN ORFNames=TRIUR3_23795 {ECO:0000313|EMBL:EMS53577.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS53577.1};
RN [1] {ECO:0000313|EMBL:EMS53577.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
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; KD192907; EMS53577.1; -; Genomic_DNA.
DR AlphaFoldDB; M7Z105; -.
DR STRING; 4572.M7Z105; -.
DR eggNOG; KOG1252; Eukaryota.
DR OMA; CMTADTG; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050017; F:L-3-cyanoalanine synthase activity; IEA:UniProt.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 27..311
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 92
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 196..200
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 284
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 61
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 339 AA; 36409 MW; 565342700496F509 CRC64;
MERMVMRLMR NKNQSLRQLQ GAAAGGLIGR TPLVYLNRVT EGCGARVAAK LEFLQPSFSV
KDRPAISMIE DAEKKGLITP GKTTLIEPTS GNMGIGLAFM AALKGYELVL TMPSYTSLER
RVVMKAFGAQ LVLTDPAKGM GGTVRKATQL YENHPSAFML QQFENPANVQ VHYETTGPEI
WEDTLGQVDI FVMGIGSGGT VTGVGKYLKE KNPNAKIYGV EPAEANVLNG GKPGPHLITG
NGVGFKPDIL DMDIMEKVLE VKGEDAVKMA KQLALQEGLL VGISSGANTV AAIELAKRPE
NKGKLIVTVH PSAGERYLSS ALFEGLRKEA EAMQPVPVD
//
