ID C0FND4_9FIRM Unreviewed; 311 AA.
AC C0FND4;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
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:EEG95892.1};
GN ORFNames=ROSEINA2194_00228 {ECO:0000313|EMBL:EEG95892.1};
OS Roseburia inulinivorans DSM 16841.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=622312 {ECO:0000313|EMBL:EEG95892.1, ECO:0000313|Proteomes:UP000003561};
RN [1] {ECO:0000313|EMBL:EEG95892.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG95892.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG95892.1, ECO:0000313|Proteomes:UP000003561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16841 {ECO:0000313|EMBL:EEG95892.1,
RC ECO:0000313|Proteomes:UP000003561};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Roseburia inulinivorans (DSM 16841).";
RL Submitted (MAR-2009) 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}.
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:EEG95892.1}.
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DR EMBL; ACFY01000009; EEG95892.1; -; Genomic_DNA.
DR RefSeq; WP_007882287.1; NZ_JAJFOJ010000001.1.
DR AlphaFoldDB; C0FND4; -.
DR GeneID; 75161379; -.
DR eggNOG; COG0031; Bacteria.
DR UniPathway; UPA00136; UER00200.
DR Proteomes; UP000003561; 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: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 10..298
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 48
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR605856-51"
SQ SEQUENCE 311 AA; 32008 MW; F3B1C4D81DEBFEB7 CRC64;
MSDIKSSTLE LVGKTPIVNA SRYAAKAGVT DATILVKLEA FNPAGSVKDR IALAMIEDAE
KKGILKEGAT IIEPTSGNTG IGLAAVAAVK GYRAILTLPD TMSVERRNLL KAYGAELVLT
EGAKGMKGAI AKADELAKEI PGAVILGQFV NPANPAAHKA TTGPEIWEQT GGKVDIFVAG
VGTGGTITGV GEYLKEQNPN VKVVAVEPAT SAVLSTGKAG AHKIQGIGAG FVPDTLNTTV
YDEIIPIENE DAFDEGRAFA VSEGVLVGIS SGAALKAATI LAKRPENKGK NIVVLLPDSG
DRYLSTALFS N
//
