METXA_MYCTA
ID METXA_MYCTA Reviewed; 379 AA.
AC A5U815;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=MRA_3382;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
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}.
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DR EMBL; CP000611; ABQ75165.1; -; Genomic_DNA.
DR RefSeq; WP_003417458.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U815; -.
DR SMR; A5U815; -.
DR STRING; 419947.MRA_3382; -.
DR ESTHER; myctu-metx; Homoserine_transacetylase.
DR EnsemblBacteria; ABQ75165; ABQ75165; MRA_3382.
DR KEGG; mra:MRA_3382; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_0_11; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000001988; 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:0016787; F:hydrolase activity; IEA:UniProt.
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; Transferase.
FT CHAIN 1..379
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_1000021888"
FT DOMAIN 52..356
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 320
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 350
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 379 AA; 39769 MW; 6F3506E4CC094D43 CRC64;
MTISDVPTQT LPAEGEIGLI DVGSLQLESG AVIDDVCIAV QRWGKLSPAR DNVVVVLHAL
TGDSHITGPA GPGHPTPGWW DGVAGPGAPI DTTRWCAVAT NVLGGCRGST GPSSLARDGK
PWGSRFPLIS IRDQVQADVA ALAALGITEV AAVVGGSMGG ARALEWVVGY PDRVRAGLLL
AVGARATADQ IGTQTTQIAA IKADPDWQSG DYHETGRAPD AGLRLARRFA HLTYRGEIEL
DTRFANHNQG NEDPTAGGRY AVQSYLEHQG DKLLSRFDAG SYVILTEALN SHDVGRGRGG
VSAALRACPV PVVVGGITSD RLYPLRLQQE LADLLPGCAG LRVVESVYGH DGFLVETEAV
GELIRQTLGL ADREGACRR