ID A0A498IH41_MALDO Unreviewed; 661 AA.
AC A0A498IH41;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN ORFNames=DVH24_036740 {ECO:0000313|EMBL:RXH82399.1};
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 {ECO:0000313|EMBL:RXH82399.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH82399.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH82399.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|ARBA:ARBA00007103,
CC ECO:0000256|RuleBase:RU003985}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH82399.1}.
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DR EMBL; RDQH01000338; RXH82399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498IH41; -.
DR STRING; 3750.A0A498IH41; -.
DR Proteomes; UP000290289; Chromosome 12.
DR GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR CDD; cd01561; CBS_like; 2.
DR Gene3D; 3.40.50.1100; -; 4.
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; 2.
DR NCBIfam; TIGR01136; cysKM; 2.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF245; CYSTEINE SYNTHASE; 1.
DR Pfam; PF00291; PALP; 2.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 2.
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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW ECO:0000256|RuleBase:RU003985};
KW Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 28..315
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT DOMAIN 336..636
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 96
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 200..204
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 288
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 65
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 661 AA; 69962 MW; 59F156C7C7DCA847 CRC64;
MEMVIGVVGC LIYLVKMVEE KSGIAKDVTE LIGQTPLVYL NRVVDGCVAK IAAKLEMMEP
CSSVKDRIGY SMIKDAEEKG LITPGESVLI EPTSGNTGIG LAFMAAAKGY KLIITMPASM
SLERRTILRG FGAELVLTDP ARGMKGAVQK AEEIVAKTPN AYMLQQFENP ANPKVHYETT
GPEIWKGSGG KVDAFVSGIG TGGTITGVGK YLKEQNPDIK LYGVEPVESA VLSGGKPGPH
KIQGIGAGFI PGVLDVNLID KVIQVTSEVA IETAKLLALK EGLLVGISSG AAAAAAIEIA
KRPENAGKLI VVVFPSFGER YLSSVLFESV KREAESMLIG NTPMVYLNNV VDGCVARIAA
KLETMEPCSS VKDRHQGMWS LSQILLCRIA YSMIKDAEDK GLITPGETVL VEPTSGNTGI
GLAFLAASKG YKLKLSMPSI VSLERRIVLR AFGAEVYITD PAKGIKGVFD KAEELLSNTP
NSHMLCQFEN PANPKIHYET TGPEIWRDSG GKVDALVAGI GTGGTVTGAG KFLKEKNSDI
KVYGVEPAES AVLNGGTPGM HLIQGIGAGF IPKVLDVSLL DEVIQVSSEE AIKTSKLLAL
KEGLLVGISS GAAAAAGIKL AKRQENAGKL IVVVFPSFGE RHLSTALFDS IRLDAENMKF
D
//
