METXA_SOLM1
ID METXA_SOLM1 Reviewed; 397 AA.
AC C4XNQ9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
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, ECO:0000303|PubMed:28581482};
GN Synonyms=metX {ECO:0000312|EMBL:BAH75060.1};
GN OrderedLocusNames=DMR_15680 {ECO:0000312|EMBL:BAH75060.1};
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:28581482}.
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:28581482};
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}.
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DR EMBL; AP010904; BAH75060.1; -; Genomic_DNA.
DR RefSeq; WP_015860266.1; NC_012796.1.
DR AlphaFoldDB; C4XNQ9; -.
DR SMR; C4XNQ9; -.
DR STRING; 573370.DMR_15680; -.
DR EnsemblBacteria; BAH75060; BAH75060; DMR_15680.
DR KEGG; dma:DMR_15680; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_7; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000009071; 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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..397
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000440280"
FT DOMAIN 58..368
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 164
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 331
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 364
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 397 AA; 43486 MW; A8CF3E6959FC4D04 CRC64;
MSEYIEHSPS GTSVGRVEKR FFTVAEADSP LTVESGRALG PVVLAYETCG QLNERADNAV
LVLHALTGDS HAAGYYEPGD AKPGWWDLMI GPGKPIDTDR YYVICSNVIG GCMGSTGPSS
LDPATGQPYG LTFPVITIGD MVRAQKRLVE HLGVTKLLSV VGGSMGGMQA LEWSVRYPDM
VRTAVPLATT TKHSALAIAF NEVARQAIMA DPNWNGGNYY DGVPPAHGLA VGRMIGHITY
LSDEAMRQKF DRRLQDRCEN SFVLEEPDFQ VESYLRYQGQ KFVDRFDANS FLYITKAADY
FNLEASHGCG SAVAAFAKAK CRYLVASFSS DWLYPTYQSR SMVQAMKKNG LDVSFVELEA
KWGHDAFLLP NARLSGMIAR FLDRALVDAA KEDARAL
