DCSD_STRLA
ID DCSD_STRLA Reviewed; 324 AA.
AC D2Z027;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=O-ureido-L-serine synthase;
DE EC=2.6.99.3;
DE AltName: Full=Cysteine synthase homolog DscD;
DE EC=2.5.1.47;
DE AltName: Full=O-acetylserine sulfhydrylase;
GN Name=dcsD;
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN CYCLOSERINE
RP BIOSYNTHESIS.
RC STRAIN=ATCC 11924;
RX PubMed=20086163; DOI=10.1128/aac.01226-09;
RA Kumagai T., Koyama Y., Oda K., Noda M., Matoba Y., Sugiyama M.;
RT "Molecular cloning and heterologous expression of a biosynthetic gene
RT cluster for the antitubercular agent D-cycloserine produced by Streptomyces
RT lavendulae.";
RL Antimicrob. Agents Chemother. 54:1132-1139(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, AND SUBUNIT.
RX PubMed=23529730; DOI=10.1128/aac.02291-12;
RA Uda N., Matoba Y., Kumagai T., Oda K., Noda M., Sugiyama M.;
RT "Establishment of an in vitro D-cycloserine-synthesizing system by using O-
RT ureido-L-serine synthase and D-cycloserine synthetase found in the
RT biosynthetic pathway.";
RL Antimicrob. Agents Chemother. 57:2603-2612(2013).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine
CC (DCS), a cyclic structural analog of D-alanine, used as an
CC antitubercular agent. Catalyzes the addition of hydroxyurea on O-
CC acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as
CC the second substrate, followed by hydroxyurea, L-homocysteine, and
CC thiosulfate. {ECO:0000269|PubMed:20086163,
CC ECO:0000269|PubMed:23529730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydroxyurea + O-acetyl-L-serine = acetate + H(+) + O-ureido-L-
CC serine; Xref=Rhea:RHEA:36263, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:44423, ChEBI:CHEBI:58340, ChEBI:CHEBI:73389; EC=2.6.99.3;
CC Evidence={ECO:0000269|PubMed:23529730};
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:0000269|PubMed:23529730};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:23529730};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 mM for OAS {ECO:0000269|PubMed:23529730};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23529730}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AB516431; BAI70378.1; -; Genomic_DNA.
DR PDB; 3X43; X-ray; 2.25 A; A/B/C/D/E/F/G/H=1-324.
DR PDB; 3X44; X-ray; 1.90 A; A/B=1-324.
DR PDBsum; 3X43; -.
DR PDBsum; 3X44; -.
DR AlphaFoldDB; D2Z027; -.
DR SMR; D2Z027; -.
DR KEGG; ag:BAI70378; -.
DR BioCyc; MetaCyc:MON-18016; -.
DR BRENDA; 2.5.1.47; 133.
DR BRENDA; 2.6.99.3; 133.
DR GO; GO:0004124; F:cysteine synthase activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
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; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01139; cysK; 1.
DR TIGRFAMs; TIGR01136; cysKM; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Antibiotic biosynthesis;
KW Cysteine biosynthesis; Pyridoxal phosphate; Transferase.
FT CHAIN 1..324
FT /note="O-ureido-L-serine synthase"
FT /id="PRO_0000424057"
FT BINDING 73
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 177..181
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3X43"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:3X44"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3X43"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 244..257
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:3X44"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:3X44"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3X43"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:3X44"
FT HELIX 312..319
FT /evidence="ECO:0007829|PDB:3X44"
SQ SEQUENCE 324 AA; 34592 MW; 944E6D1CEEFBB69F CRC64;
MPLFNSILDT IGRTPIVRLQ RMAPEHTSVY VKVESFNPGG SVKDRLALSV VLDAEAKGLL
KPGDTIVECT SGNVGIALAM VAAARGYRFV AVMGDTYSVE RRKLIRAYGG KLVLFPGHLG
SKGGNLIADE LAEKYGWFRA RQFDNPANPS YHRETTASEI LADFAGKRLD HFVTGFGTTG
TLTGVGQMLR VARPEVRVVA LEPSNAAMLA RGEWSPHQIQ GLAPNFVPGV LDRSVIDDLV
TMDEVTARDT SRRLAAEEGI FAGISAGATV ATALSIAEHA PEGTVLLAML PDTGERYLST
FLFDGVDEGS DDAWLASLDT GSGL
