METXA_CORGL
ID METXA_CORGL Reviewed; 377 AA.
AC O68640;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:9666465};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482, ECO:0000303|PubMed:9666465};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482, ECO:0000269|PubMed:9666465};
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=metA {ECO:0000303|PubMed:9666465};
GN OrderedLocusNames=Cgl0652, cg0754;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=9666465;
RA Park S.-D., Lee J.-Y., Kim Y., Kim J.-H., Lee H.-S.;
RT "Isolation and analysis of metA, a methionine biosynthetic gene encoding
RT homoserine acetyltransferase in Corynebacterium glutamicum.";
RL Mol. Cells 8:286-294(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
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, ECO:0000269|PubMed:9666465}.
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, ECO:0000269|PubMed:9666465};
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, ECO:0000269|PubMed:9666465}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot grow on minimal media with no added
CC methionine. {ECO:0000269|PubMed:9666465}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; AF052652; AAC06035.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98045.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19358.1; -; Genomic_DNA.
DR RefSeq; NP_599885.1; NC_003450.3.
DR RefSeq; WP_011013793.1; NC_006958.1.
DR AlphaFoldDB; O68640; -.
DR SMR; O68640; -.
DR STRING; 196627.cg0754; -.
DR ESTHER; corgl-metx; Homoserine_transacetylase.
DR World-2DPAGE; 0001:O68640; -.
DR KEGG; cgb:cg0754; -.
DR KEGG; cgl:Cgl0652; -.
DR PATRIC; fig|196627.13.peg.638; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_0_11; -.
DR OMA; TRFCVVS; -.
DR BioCyc; MetaCyc:MON-9447; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000582; 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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..377
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155715"
FT DOMAIN 48..347
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 341
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT CONFLICT 139
FT /note="V -> VVL (in Ref. 1; AAC06035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41178 MW; F06AC59ECF205024 CRC64;
MPTLAPSGQL EIQAIGDVST EAGAIITNAE IAYHRWGEYR VDKEGRSNVV LIEHALTGDS
NAADWWADLL GPGKAINTDI YCVICTNVIG GCNGSTGPGS MHPDGNFWGN RFPATSIRDQ
VNAEKQFLDA LGITTVAAVL GGSMGGARTL EWAAMYPETV GAAAVLAVSA RASAWQIGIQ
SAQIKAIEND HHWHEGNYYE SGCNPATGLG AARRIAHLTY RGELEIDERF GTKAQKNENP
LGPYRKPDQR FAVESYLDYQ ADKLVQRFDA GSYVLLTDAL NRHDIGRDRG GLNKALESIK
VPVLVAGVDT DILYPYHQQE HLSRNLGNLL AMAKIVSPVG HDAFLTESRQ MDRIVRNFFS
LISPDEDNPS TYIEFYI
