METXA_MYCTU
ID METXA_MYCTU Reviewed; 379 AA.
AC P9WJY9; L0TDV2; O53391; P0A5J8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
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}; Synonyms=metA;
GN OrderedLocusNames=Rv3341; ORFNames=MTV016.41;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP46162.1; -; Genomic_DNA.
DR PIR; D70846; D70846.
DR RefSeq; NP_217858.1; NC_000962.3.
DR RefSeq; WP_003417458.1; NZ_NVQJ01000051.1.
DR PDB; 6PUX; X-ray; 1.90 A; A/B=10-372.
DR PDBsum; 6PUX; -.
DR AlphaFoldDB; P9WJY9; -.
DR SMR; P9WJY9; -.
DR STRING; 83332.Rv3341; -.
DR ESTHER; myctu-metx; Homoserine_transacetylase.
DR PaxDb; P9WJY9; -.
DR GeneID; 888030; -.
DR KEGG; mtu:Rv3341; -.
DR TubercuList; Rv3341; -.
DR eggNOG; COG2021; Bacteria.
DR OMA; TRFCVVS; -.
DR PhylomeDB; P9WJY9; -.
DR BRENDA; 2.3.1.31; 3445.
DR UniPathway; UPA00051; UER00074.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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..379
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155731"
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"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 32..44
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:6PUX"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6PUX"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 220..234
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:6PUX"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:6PUX"
FT TURN 294..299
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:6PUX"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6PUX"
FT HELIX 357..371
FT /evidence="ECO:0007829|PDB:6PUX"
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
