DCSG_STRLA
ID DCSG_STRLA Reviewed; 299 AA.
AC D2Z030;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Cycloserine biosynthesis protein DcsG;
DE EC=6.3.3.5;
GN Name=dcsG;
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN THE CYCLOSERINE
RP BIOSYNTHESIS, AND DISRUPTION PHENOTYPE.
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, SUBSTRATE SPECIFICITY, 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 synthesis of D-cycloserine from O-
CC ureido-D-serine. It reacts exclusively with O-ureido-D-serine.
CC {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:23529730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + H2O + O-ureido-D-serine = ADP + CO2 + D-
CC cycloserine + NH4(+) + phosphate; Xref=Rhea:RHEA:36711,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:74158, ChEBI:CHEBI:75929, ChEBI:CHEBI:456216; EC=6.3.3.5;
CC Evidence={ECO:0000269|PubMed:23529730};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23529730}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not produce
CC cycloserine (DCS). {ECO:0000269|PubMed:20086163}.
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DR EMBL; AB516431; BAI70381.1; -; Genomic_DNA.
DR PDB; 6JIL; X-ray; 2.32 A; A/B/C/D=1-299.
DR PDBsum; 6JIL; -.
DR AlphaFoldDB; D2Z030; -.
DR SMR; D2Z030; -.
DR KEGG; ag:BAI70381; -.
DR BioCyc; MetaCyc:MON-18019; -.
DR BRENDA; 6.3.3.5; 133.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016882; F:cyclo-ligase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IMP:UniProtKB.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; ATP-binding; Ligase; Magnesium;
KW Manganese; Metal-binding; Nucleotide-binding.
FT CHAIN 1..299
FT /note="Cycloserine biosynthesis protein DcsG"
FT /id="PRO_0000424059"
FT DOMAIN 95..298
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 127..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6JIL"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6JIL"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6JIL"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:6JIL"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:6JIL"
SQ SEQUENCE 299 AA; 32786 MW; 8E4784DF256B9B23 CRC64;
MGILALVTDA VSLPIDYDMP PLLEACRTVG ITAEVCDWED GTVDWSRFEA VVFRSPWTWA
ERQAEFLAFC ERVSHVTRLI TPMPLVRWAL DKRYLADLAA HGVPVIPTTV VAPGSDALAA
VRDFLAARPE AREFVVKPTD GCYSKDVQRY QRSLAEPASR HVARLLANGS HVILQPYVES
VDRHGETDLT FFDGVYSHAI HKGAMLMPDG TVHVPTLDFR QARDADEDQR AVAAAALAAS
VAHLGLDLPL VCGRVDLVRG ADGSPMVLEM ELCEPSLNLT FSEDGALRFA QALAERLKP
