METAA_BACC1
ID METAA_BACC1 Reviewed; 301 AA.
AC Q72X44;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000305};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000269|PubMed:18216013};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:18216013};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00295, ECO:0000303|PubMed:18216013};
GN Name=metAA {ECO:0000255|HAMAP-Rule:MF_00295};
GN Synonyms=metA {ECO:0000303|PubMed:17546672}; OrderedLocusNames=BCE_5534;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
RN [2]
RP 3D-STRUCTURE MODELING.
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).
RN [3] {ECO:0007744|PDB:2GHR}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=17546672; DOI=10.1002/prot.21208;
RA Zubieta C., Krishna S.S., McMullan D., Miller M.D., Abdubek P.,
RA Agarwalla S., Ambing E., Astakhova T., Axelrod H.L., Carlton D., Chiu H.J.,
RA Clayton T., Deller M., DiDonato M., Duan L., Elsliger M.A., Grzechnik S.K.,
RA Hale J., Hampton E., Han G.W., Haugen J., Jaroszewski L., Jin K.K.,
RA Klock H.E., Knuth M.W., Koesema E., Kumar A., Marciano D., Morse A.T.,
RA Nigoghossian E., Oommachen S., Reyes R., Rife C.L., van den Bedem H.,
RA Weekes D., White A., Xu Q., Hodgson K.O., Wooley J., Deacon A.M.,
RA Godzik A., Lesley S.A., Wilson I.A.;
RT "Crystal structure of homoserine O-succinyltransferase from Bacillus cereus
RT at 2.4 A resolution.";
RL Proteins 68:999-1005(2007).
RN [4] {ECO:0007744|PDB:2VDJ}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L-HOMOSERINE,
RP FUNCTION AS AN ACETYLTRANSFERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF LYS-47;
RP GLU-111; CYS-142; LYS-163; SER-192; HIS-235; GLU-237 AND ARG-249.
RX PubMed=18216013; DOI=10.1074/jbc.m709283200;
RA Zubieta C., Arkus K.A., Cahoon R.E., Jez J.M.;
RT "A single amino acid change is responsible for evolution of acyltransferase
RT specificity in bacterial methionine biosynthesis.";
RL J. Biol. Chem. 283:7561-7567(2008).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in
CC which the acetyl group of acetyl-CoA is initially transferred to the
CC enzyme to form an acetyl-enzyme intermediate before subsequent transfer
CC to homoserine to form the final product, O-acetylhomoserine. Cannot use
CC succinyl-CoA as the acyl donor. {ECO:0000269|PubMed:18216013}.
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_00295,
CC ECO:0000269|PubMed:18216013};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=185 uM for acetyl-CoA {ECO:0000269|PubMed:18216013};
CC KM=214 uM for homoserine {ECO:0000269|PubMed:18216013};
CC Note=kcat is 58.6 min(-1). {ECO:0000269|PubMed:18216013};
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_00295, ECO:0000305|PubMed:18216013}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17546672,
CC ECO:0000269|PubMed:18216013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00295,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MetA family. {ECO:0000255|HAMAP-
CC Rule:MF_00295}.
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DR EMBL; AE017194; AAS44434.1; -; Genomic_DNA.
DR RefSeq; WP_001121522.1; NC_003909.8.
DR PDB; 2GHR; X-ray; 2.40 A; A=1-301.
DR PDB; 2VDJ; X-ray; 2.00 A; A=1-301.
DR PDBsum; 2GHR; -.
DR PDBsum; 2VDJ; -.
DR AlphaFoldDB; Q72X44; -.
DR SMR; Q72X44; -.
DR DNASU; 2750729; -.
DR EnsemblBacteria; AAS44434; AAS44434; BCE_5534.
DR GeneID; 59156897; -.
DR KEGG; bca:BCE_5534; -.
DR HOGENOM; CLU_057851_0_1_9; -.
DR OMA; WLWFCYQ; -.
DR BRENDA; 2.3.1.46; 648.
DR UniPathway; UPA00051; UER00074.
DR EvolutionaryTrace; Q72X44; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019281; P:L-methionine biosynthetic process from homoserine via O-succinyl-L-homoserine and cystathionine; IEA:InterPro.
DR CDD; cd03131; GATase1_HTS; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00295; MetA_acyltransf; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005697; HST_MetA.
DR InterPro; IPR033752; MetA_family.
DR PANTHER; PTHR20919; PTHR20919; 1.
DR Pfam; PF04204; HTS; 1.
DR PIRSF; PIRSF000450; H_ser_succinyltr; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01001; metA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..301
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000199736"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013"
FT ACT_SITE 237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000305|PubMed:17546672, ECO:0000305|PubMed:18216013"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000269|PubMed:18216013, ECO:0007744|PDB:2VDJ"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000269|PubMed:18216013, ECO:0007744|PDB:2VDJ"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295,
FT ECO:0000269|PubMed:18216013, ECO:0007744|PDB:2VDJ"
FT SITE 111
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT SITE 192
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00295"
FT MUTAGEN 47
FT /note="K->M: 17-fold increase in Km for acetyl-CoA and 14-
FT fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 47
FT /note="K->R: 7-fold increase in Km for acetyl-CoA."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 111
FT /note="E->G: No activity with acetyl-CoA but catalyzes an
FT acyltransferase reaction using succinyl-CoA and
FT homoserine."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 142
FT /note="C->A,S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 163
FT /note="K->M: 13-fold increase in Km for homoserine."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 192
FT /note="S->A: 5-fold increase in Km for homoserine."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 235
FT /note="H->A,N,Q: Lack of activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 237
FT /note="E->A: 65-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 237
FT /note="E->D: 6-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 237
FT /note="E->Q: 19-fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT MUTAGEN 249
FT /note="R->M: 64-fold increase in Km for homoserine and 10-
FT fold decrease in catalytic activity."
FT /evidence="ECO:0000269|PubMed:18216013"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2VDJ"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 143..153
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 158..172
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 185..196
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2VDJ"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2VDJ"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2VDJ"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:2VDJ"
SQ SEQUENCE 301 AA; 35340 MW; 6476C52969F5067D CRC64;
MPIIIDKDLP ARKVLQEENI FVMTKERAET QDIRALKIAI LNLMPTKQET EAQLLRLIGN
TPLQLDVHLL HMESHLSRNV AQEHLTSFYK TFRDIENEKF DGLIITGAPV ETLSFEEVDY
WEELKRIMEY SKTNVTSTLH ICWGAQAGLY HHYGVQKYPL KEKMFGVFEH EVREQHVKLL
QGFDELFFAP HSRHTEVRES DIREVKELTL LANSEEAGVH LVIGQEGRQV FALGHSEYSC
DTLKQEYERD RDKGLNIDVP KNYFKHDNPN EKPLVRWRSH GNLLFSNWLN YYVYQETPYV
L
