METXA_HAEIN
ID METXA_HAEIN Reviewed; 358 AA.
AC P45131;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
DE Short=HAT {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.31 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:10913262, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine O-trans-acetylase {ECO:0000305};
DE AltName: Full=Homoserine transacetylase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:10913262};
DE Short=HTA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
GN Name=metXA {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN Synonyms=met2; OrderedLocusNames=HI_1263;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND PROTEIN SEQUENCE OF
RP 2-11.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, BIOPHYSICOCHEMICAL
RP PROPERTIES, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=10913262; DOI=10.1021/bi000462p;
RA Born T.L., Franklin M., Blanchard J.S.;
RT "Enzyme-catalyzed acylation of homoserine: mechanistic characterization of
RT the Haemophilus influenzae met2-encoded homoserine transacetylase.";
RL Biochemistry 39:8556-8564(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP LEU-306, AND 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 [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), ACTIVE SITE, AND SUBUNIT.
RX PubMed=16313180; DOI=10.1021/bi051951y;
RA Mirza I.A., Nazi I., Korczynska M., Wright G.D., Berghuis A.M.;
RT "Crystal structure of homoserine transacetylase from Haemophilus influenzae
RT reveals a new family of alpha/beta-hydrolases.";
RL Biochemistry 44:15768-15773(2005).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine (PubMed:10913262, PubMed:28581482).
CC Utilizes a ping-pong kinetic mechanism in which the acetyl group of
CC acetyl-CoA is initially transferred to the enzyme to form an acetyl-
CC enzyme intermediate before subsequent transfer to homoserine to form
CC the final product, O-acetylhomoserine (PubMed:10913262).
CC {ECO:0000269|PubMed:10913262, ECO:0000269|PubMed:28581482}.
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:10913262, ECO:0000269|PubMed:28581482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for L-homoserine (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=570 uM for L-homoserine {ECO:0000269|PubMed:28581482};
CC KM=140 uM for acetyl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=586 uM for acetyl-CoA {ECO:0000269|PubMed:28581482};
CC KM=90 uM for propionyl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=130 uM for crotonyl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=210 uM for butyryl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=280 uM for glutaryl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=360 uM for succinyl-CoA (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC KM=1400 uM for 4-nitrophenyl acetate (at 25 degrees Celsius and pH
CC 7.5) {ECO:0000269|PubMed:10913262};
CC KM=4700 uM for D-homoserine (at 25 degrees Celsius and pH 7.5)
CC {ECO:0000269|PubMed:10913262};
CC Note=kcat is 92 sec(-1) with acetyl-CoA and L-homoserine as
CC substrates (at 25 degrees Celsius and pH 7.5) (PubMed:10913262). kcat
CC is 5 sec(-1) (PubMed:28581482). {ECO:0000269|PubMed:10913262,
CC ECO:0000269|PubMed:28581482};
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 ECO:0000269|PubMed:10913262, ECO:0000269|PubMed:16313180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- MASS SPECTROMETRY: Mass=39859; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10913262};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; L42023; AAC22916.1; -; Genomic_DNA.
DR PIR; D64113; D64113.
DR RefSeq; NP_439418.1; NC_000907.1.
DR RefSeq; WP_005694320.1; NC_000907.1.
DR PDB; 2B61; X-ray; 1.65 A; A=1-358.
DR PDBsum; 2B61; -.
DR AlphaFoldDB; P45131; -.
DR SMR; P45131; -.
DR STRING; 71421.HI_1263; -.
DR ESTHER; haein-metx; Homoserine_transacetylase.
DR EnsemblBacteria; AAC22916; AAC22916; HI_1263.
DR KEGG; hin:HI_1263; -.
DR PATRIC; fig|71421.8.peg.1315; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR PhylomeDB; P45131; -.
DR BioCyc; HINF71421:G1GJ1-1291-MON; -.
DR BRENDA; 2.3.1.31; 2529.
DR UniPathway; UPA00051; UER00074.
DR EvolutionaryTrace; P45131; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IDA:UniProtKB.
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 Direct protein sequencing; Methionine biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7542800"
FT CHAIN 2..358
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155719"
FT DOMAIN 41..343
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 ECO:0000305|PubMed:16313180"
FT ACT_SITE 304
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:16313180"
FT ACT_SITE 337
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:16313180"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
FT MUTAGEN 306
FT /note="L->R: Can no longer use acetyl-CoA as acyl donor,
FT but can use succinyl-CoA."
FT /evidence="ECO:0000269|PubMed:28581482"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2B61"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2B61"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:2B61"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:2B61"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 309..321
FT /evidence="ECO:0007829|PDB:2B61"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2B61"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:2B61"
SQ SEQUENCE 358 AA; 39990 MW; 2484D6BEAC761983 CRC64;
MSVQNVVLFD TQPLTLMLGG KLSHINVAYQ TYGTLNAEKN NAVLICHALT GDAEPYFDDG
RDGWWQNFMG AGLALDTDRY FFISSNVLGG CKGTTGPSSI NPQTGKPYGS QFPNIVVQDI
VKVQKALLDH LGISHLKAII GGSFGGMQAN QWAIDYPDFM DNIVNLCSSI YFSAEAIGFN
HVMRQAVIND PNFNGGDYYE GTPPDQGLSI ARMLGMLTYR TDLQLAKAFG RATKSDGSFW
GDYFQVESYL SYQGKKFLER FDANSYLHLL RALDMYDPSL GYDNVKEALS RIKARYTLVS
VTTDQLFKPI DLYKSKQLLE QSGVDLHFYE FPSDYGHDAF LVDYDQFEKR IRDGLAGN
