ID Q70E79_CORGT Unreviewed; 377 AA.
AC Q70E79;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
DE Short=HAT {ECO:0000256|HAMAP-Rule:MF_00296};
DE EC=2.3.1.31 {ECO:0000256|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine transacetylase {ECO:0000256|HAMAP-Rule:MF_00296};
DE Short=HTA {ECO:0000256|HAMAP-Rule:MF_00296};
GN Name=metA {ECO:0000313|EMBL:CAE48280.1};
GN Synonyms=metXA {ECO:0000256|HAMAP-Rule:MF_00296};
GN ORFNames=BBD29_03690 {ECO:0000313|EMBL:ANU32926.1};
OS Corynebacterium glutamicum (Brevibacterium saccharolyticum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1718 {ECO:0000313|EMBL:CAE48280.1};
RN [1] {ECO:0000313|EMBL:CAE48280.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TK3600 {ECO:0000313|EMBL:CAE48280.1};
RA Bui Thi H., Vu Thi H., Le Lan H., Trinh Quy B., Nguyen Tien M.,
RA Bach Thi Q.N., Nguyen Thuy C., Dinh Duy K.;
RT "Cloning of the gene coding for homoserine acetyltransferase from
RT Corynebacterium glutamicum isolate TK3600.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13869 {ECO:0000313|Proteomes:UP000092697};
RA Chen X., Yang J., Jiang Y., Yang S., Zhang Y.;
RT "Genome sequence of Corynebacterium glutamicum ATCC 13869.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ANU32926.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 13869 {ECO:0000313|EMBL:ANU32926.1};
RX PubMed=28198668;
RA Yang J., Yang S.;
RT "Comparative analysis of Corynebacterium glutamicum genomes: a new
RT perspective for the industrial production of amino acids.";
RL BMC Genomics 18:940-940(2017).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR EMBL; CP016335; ANU32926.1; -; Genomic_DNA.
DR EMBL; AJ584663; CAE48280.1; -; Genomic_DNA.
DR RefSeq; WP_003860777.1; NZ_LOQY01000069.1.
DR AlphaFoldDB; Q70E79; -.
DR ESTHER; corgl-metx; Homoserine_transacetylase.
DR KEGG; cgx:SB89_03465; -.
DR PATRIC; fig|1718.46.peg.739; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000092697; 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; alpha/beta hydrolase; 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 NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 48..347
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 143
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 311
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 341
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 377 AA; 41216 MW; 79BC53BE4F433F2E CRC64;
MPTLAPSGQL EIQAIGDVST EAGAIIKNAE IAYHRWGEYR VDKEGRSNVV LIEHALTGDS
NAADWWADLL GPGKAINTDI YCVICTNVIG GCNGSTGPGS MHPDGNFWGN RFPATSIRDQ
VNAEKQFLDA LGITTVAAVL GGSMGGARTL EWAAMYPEIV GAAAVLAVSA RASAWQIGIQ
SAQIKAIEND HHWHEGNYYE SGCNPATGLG AARRIAHLTY RGELEIDERF GTKAQKNENP
LGPYRKPDQR FAVESYLDYQ ADKLVQRFDA GSYVLLTDAL NRHDIGRDRG GLNKALESIK
VPVLVAGVDT DILYPYHQQE HLSRNLGNLL AMAKIVSPVG HDAFLTESRQ MDRIVRNFFS
LISPDENNPS TYIEFYI
//
