METXA_DESPS
ID METXA_DESPS Reviewed; 390 AA.
AC Q6ANV2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296}; OrderedLocusNames=DP1243;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAG35972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR522870; CAG35972.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041277703.1; NC_006138.1.
DR AlphaFoldDB; Q6ANV2; -.
DR SMR; Q6ANV2; -.
DR STRING; 177439.DP1243; -.
DR ESTHER; desps-q6anv2; Homoserine_transacetylase.
DR MEROPS; S33.A02; -.
DR EnsemblBacteria; CAG35972; CAG35972; DP1243.
DR KEGG; dps:DP1243; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_7; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009086; P:methionine biosynthetic process; 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 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..390
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155717"
FT DOMAIN 55..366
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 163
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 329
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 362
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 390 AA; 43329 MW; FC64FBE69C6CFFA3 CRC64;
MEKEIKDHKS VGIVEKQFFT CAQVPSPLIL ENGAKLGPIT IAYETYGNLS ARKDNAILIN
HAFSGDSHVA GHYATDGPKE KPGWWDFLVG PGKGIDTDKY FIICSNILGS CNGTTGPASK
NSETGEAYAL DFPMVTIGDM VATQKLLIDH LGIPKLLAVI GGSVGGMQTL EWAIRYPEMM
HSVIPIATTM RHSALAIAFN EIARQAIMTD PHWNRGKYYG QAHPDTGLAV ARMVGHVTYL
SDEAMRRKFG RNLQEKENLS YGFDADFQVE SYLRYQGNKF VHRFDANSLL YITKASDYFD
IVERISTSGP ETELTAPQQK YLVISYSSDW LYPTYQARDL VKALKRSGRN VSFSEIESDC
GHDAFLIPDD RLEQLMRGFL AGIYTGIAEI
