DCSE_STRLA
ID DCSE_STRLA Reviewed; 374 AA.
AC D2Z028;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=L-serine/homoserine O-acetyltransferase;
DE EC=2.3.1.30;
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine O-trans-acetylase {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=dcsE; Synonyms=metX;
OS Streptomyces lavendulae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
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 X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF WILD-TYPE AND MUTANTS, FUNCTION,
RP MUTAGENESIS OF GLY-52 AND PRO-55, ACTIVE SITE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=23396912; DOI=10.1128/jb.02085-12;
RA Oda K., Matoba Y., Kumagai T., Noda M., Sugiyama M.;
RT "Crystallographic study to determine the substrate specificity of an L-
RT serine-acetylating enzyme found in the D-cycloserine biosynthetic
RT pathway.";
RL J. Bacteriol. 195:1741-1749(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 transfer of the acetyl group from
CC acetyl-CoA to the hydroxyl group of L-serine to yield the activated
CC serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine.
CC {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:23396912}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine;
CC Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30;
CC Evidence={ECO:0000269|PubMed:20086163};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine;
CC Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:20086163};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.9 mM for L-serine (at 30 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:23396912};
CC KM=98 mM for L-homoserine (at 30 degrees Celsius and pH 8)
CC {ECO:0000269|PubMed:23396912};
CC Note=kcat is 95 min(-1) and 88 min(-1) for L-serine and L-homoserine,
CC respectively (at 30 degrees Celsius and pH 8).;
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:20086163}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:23396912}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB516431; BAI70379.1; -; Genomic_DNA.
DR PDB; 3VVL; X-ray; 1.81 A; A/B=1-374.
DR PDB; 3VVM; X-ray; 1.70 A; A/B=1-374.
DR PDBsum; 3VVL; -.
DR PDBsum; 3VVM; -.
DR AlphaFoldDB; D2Z028; -.
DR SMR; D2Z028; -.
DR ESTHER; strla-d2z028; Homoserine_transacetylase.
DR PRIDE; D2Z028; -.
DR KEGG; ag:BAI70379; -.
DR BioCyc; MetaCyc:MON-18015; -.
DR BRENDA; 2.3.1.30; 133.
DR BRENDA; 2.3.1.31; 133.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016750; F:O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Transferase.
FT CHAIN 1..374
FT /note="L-serine/homoserine O-acetyltransferase"
FT /id="PRO_0000424058"
FT DOMAIN 46..357
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 319
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 352
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 52
FT /note="Important for substrate specificity"
FT SITE 55
FT /note="Important for substrate specificity"
FT MUTAGEN 52
FT /note="G->A: Has much lower activity for the acetylation of
FT L-serine but keeps the activity against L-homoserine.
FT Utilizes L-homoserine as a substrate for acetylation but
FT barely utilizes L-serine; when associated with G-55."
FT /evidence="ECO:0000269|PubMed:23396912"
FT MUTAGEN 55
FT /note="P->G: Can acetylate both L-serine and L-homoserine.
FT Utilizes L-homoserine as a substrate for acetylation but
FT barely utilizes L-serine; when associated with A-52."
FT /evidence="ECO:0000269|PubMed:23396912"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3VVM"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3VVM"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3VVM"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:3VVL"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 274..286
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:3VVM"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:3VVM"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:3VVM"
SQ SEQUENCE 374 AA; 40268 MW; 1199AAFDC0D969CD CRC64;
MREFIPPASR FIELPDGFAM RRGGALYGAR IAYETFGSLN AARDNAVLVL TGLSPDAHAA
SRPDDPTPGW WEAMVGPGKP VDTDLWHVIC VNSLGSCKGS TGPASTDPRT GEPYRLSFPE
LSIEDIADAA AHTVRALGIS RLACVVGASM GGMSALALLA RHPELARTHI SLSGAVHALP
FSIAVRSLQR EAIRSDPGWL QGHYDEGEGP RRGMLTARKL GMMTYRSAQE WDCRFGRTRI
GERRRADQGR FGPEFEVESY LDFHAQRFAD RFDPNSYLYL SHAMDQFDLG DGGGGGGGAP
GALSRMRVER ALVMGARTDI LFPLSQQQEI ADGLSAGGAD VSFLPVDTPA GHDAFLVDIE
RFGPPVAKFL AIVA
