ID E3N127_CAERE Unreviewed; 337 AA.
AC E3N127;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Cysteine synthase {ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|RuleBase:RU003985};
GN ORFNames=CRE_12976 {ECO:0000313|EMBL:EFO83107.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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}.
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DR EMBL; DS268507; EFO83107.1; -; Genomic_DNA.
DR RefSeq; XP_003097850.1; XM_003097802.1.
DR AlphaFoldDB; E3N127; -.
DR STRING; 31234.E3N127; -.
DR EnsemblMetazoa; CRE12976.1; CRE12976.1; WBGene00067605.
DR GeneID; 9826998; -.
DR KEGG; crq:GCK72_020688; -.
DR CTD; 9826998; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_1_0_1; -.
DR InParanoid; E3N127; -.
DR OMA; KFADDEW; -.
DR OrthoDB; 852805at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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; 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; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF71; CYSTEINE SYNTHASE-RELATED; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR605856-50,
KW ECO:0000256|RuleBase:RU003985};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 13..295
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 78
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 182..186
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 270
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 47
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 337 AA; 36536 MW; 18A12A15344029DA CRC64;
MSRQTMVADG GETIGNTPLV LLRNIPKGTD ARIAVKIEYL NPSCSVKDRI AKSMVEEAEK
AGRIVPGRTV LVEGTSGNLG IALAHIGKIR GYKVILVMPE TMSVERRAML RAYGAEVILS
DPMEGHPGVI KKVEMLCEKL PNAICLDQFS NPANPAAHYR TTGPEIWRQT DGKVDMVCFG
VGSSGTLTGV GRYLRQQNPD IKIYPVEPYE SSVLSGFPRG KHRIQGIGAG IIPGNVDRSL
FTEVLRVTSD DAMTMARRLA DEEAILGGIS SGANVVAAMQ LASRPENKGK LIVTTVNSFA
ERYFTTELYS NVLNDVSKLK WSNDDEAVAI AKKYLGI
//