METXA_MYCS2
ID METXA_MYCS2 Reviewed; 380 AA.
AC A0QSZ0; I7F941;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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};
GN OrderedLocusNames=MSMEG_1651, MSMEI_1613;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK71400.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP38085.1; -; Genomic_DNA.
DR RefSeq; WP_011727801.1; NC_018289.1.
DR RefSeq; YP_886028.1; NC_008596.1.
DR PDB; 6IOG; X-ray; 1.55 A; A/B=14-380.
DR PDB; 6IOH; X-ray; 2.00 A; A/B=14-380.
DR PDB; 6IOI; X-ray; 1.60 A; A/B=14-380.
DR PDBsum; 6IOG; -.
DR PDBsum; 6IOH; -.
DR PDBsum; 6IOI; -.
DR AlphaFoldDB; A0QSZ0; -.
DR SMR; A0QSZ0; -.
DR STRING; 246196.MSMEI_1613; -.
DR ESTHER; mycs2-metx; Homoserine_transacetylase.
DR EnsemblBacteria; ABK71400; ABK71400; MSMEG_1651.
DR EnsemblBacteria; AFP38085; AFP38085; MSMEI_1613.
DR GeneID; 66733102; -.
DR KEGG; msg:MSMEI_1613; -.
DR KEGG; msm:MSMEG_1651; -.
DR PATRIC; fig|246196.19.peg.1636; -.
DR eggNOG; COG2021; Bacteria.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..380
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_1000021885"
FT DOMAIN 59..363
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 327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 357
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 39..51
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6IOG"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6IOG"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 165..176
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:6IOG"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 244..251
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:6IOG"
FT TURN 301..306
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 308..313
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 332..341
FT /evidence="ECO:0007829|PDB:6IOG"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:6IOG"
FT HELIX 364..378
FT /evidence="ECO:0007829|PDB:6IOG"
SQ SEQUENCE 380 AA; 39954 MW; 75EE16B2AEED6F98 CRC64;
MTIIEERATD TGMATVPLPA EGEIGLVHIG ALTLENGTVL PDVTIAVQRW GELAPDRGNV
VMVLHALTGD SHVTGPAGDG HPTAGWWDGV AGPGAPIDTD HWCAIATNVL GGCRGSTGPG
SLAPDGKPWG SRFPQITIRD QVAADRAALA ALGITEVAAV VGGSMGGARA LEWLVTHPDD
VRAGLVLAVG ARATADQIGT QSTQVAAIKA DPDWQGGDYH GTGRAPTEGM EIARRFAHLT
YRGEEELDDR FANTPQDDED PLTGGRYAVQ SYLEYQGGKL ARRFDPGTYV VLSDALSSHD
VGRGRGGVEA ALRSCPVPVV VGGITSDRLY PIRLQQELAE LLPGCQGLDV VDSIYGHDGF
LVETELVGKL IRRTLELAQR
