ID Q9RAS8_LACLC Unreviewed; 306 AA.
AC Q9RAS8;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-DEC-2001, sequence version 2.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Cysteine synthase {ECO:0000256|ARBA:ARBA00019371, ECO:0000256|RuleBase:RU003985};
DE EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681, ECO:0000256|RuleBase:RU003985};
GN Name=cysK {ECO:0000313|EMBL:AAF14694.2};
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359 {ECO:0000313|EMBL:AAF14694.2};
RN [1] {ECO:0000313|EMBL:AAF14694.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MG1363 {ECO:0000313|EMBL:AAF14694.2};
RX PubMed=10618201; DOI=10.1128/AEM.66.11.5024-5029.2000;
RA Fernandez M., van Doesburg W., Rutten G.A.M., Marugg J.D., Alting A.C.,
RA van Kranenburg R., Kuipers O.P.;
RT "Molecular and functional analyses of the metC gene of Lactococcus lactis,
RT encoding cystathionine beta-lyase.";
RL Appl. Environ. Microbiol. 66:42-48(2000).
RN [2] {ECO:0000313|EMBL:AAF14694.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MG1363 {ECO:0000313|EMBL:AAF14694.2};
RA Fernandez M., van Doesburg W., Rutten G.A.M., Marugg J.D., Alting A.C.,
RA van Kranenburg R., Kuipers O.P.;
RL Submitted (SEP-2001) 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|ARBA:ARBA00000298,
CC 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 -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
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; AF131880; AAF14694.2; -; Genomic_DNA.
DR PIR; T47233; T47233.
DR RefSeq; WP_011835559.1; NZ_RIMN01000068.1.
DR AlphaFoldDB; Q9RAS8; -.
DR SMR; Q9RAS8; -.
DR PATRIC; fig|1359.42.peg.994; -.
DR OMA; MWGAEII; -.
DR UniPathway; UPA00136; UER00200.
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:SF194; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR605856-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003985}.
FT DOMAIN 8..291
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 74
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 178..182
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT BINDING 266
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-50"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 306 AA; 32751 MW; 0159F174D5B9083D CRC64;
MVKIVENITE LVGNSPIIKL KNGPENGAEI YLKLEYFNPG GSVKDRIALQ MIRQAEADGR
LKKGGTIVEP TSGNTGIGLA MAGAALGYNV VIIMPDSYSK ERRQLIQAYG AELILTPAAD
GIKAAIDLGQ KLVEENGWFM PMQFENPANL KAHELTTGPE IIEAFGENGL DAFVACAGTG
GTISGVSHYL KSQNSKIKTF VVEPAESPIL TGGESGPHRI QGIGIPFMSP NLDTEAYDRV
INVTSDEALE TARKIGKNEG FLVGISSGAA IWAAYELAKK LGKDQKVLAL CADNGERYLS
TELYDY
//
