METXA_LEPIN
ID METXA_LEPIN Reviewed; 366 AA.
AC Q8F4I0;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Homoserine O-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
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:28581482};
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, ECO:0000303|PubMed:28581482};
GN OrderedLocusNames=LA_2061;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ACTIVE SITE.
RX PubMed=17927957; DOI=10.1016/j.bbrc.2007.08.153;
RA Wang M., Liu L., Wang Y., Wei Z., Zhang P., Li Y., Jiang X., Xu H.,
RA Gong W.;
RT "Crystal structure of homoserine O-acetyltransferase from Leptospira
RT interrogans.";
RL Biochem. Biophys. Res. Commun. 363:1050-1056(2007).
CC -!- FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine,
CC forming acetyl-L-homoserine (PubMed:17927957, 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:17927957).
CC {ECO:0000269|PubMed:17927957, 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:17927957, ECO:0000269|PubMed:28581482};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for L-homoserine {ECO:0000269|PubMed:17927957};
CC KM=0.95 mM for acetyl-CoA {ECO:0000269|PubMed:17927957};
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:17927957}.
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; AE010300; AAN49260.1; -; Genomic_DNA.
DR RefSeq; NP_712242.1; NC_004342.2.
DR RefSeq; WP_001005981.1; NC_004342.2.
DR PDB; 2PL5; X-ray; 2.20 A; A=1-366.
DR PDBsum; 2PL5; -.
DR AlphaFoldDB; Q8F4I0; -.
DR SMR; Q8F4I0; -.
DR STRING; 189518.LA_2061; -.
DR ESTHER; lepin-METX; Homoserine_transacetylase.
DR EnsemblBacteria; AAN49260; AAN49260; LA_2061.
DR GeneID; 61141749; -.
DR KEGG; lil:LA_2061; -.
DR PATRIC; fig|189518.3.peg.2057; -.
DR HOGENOM; CLU_028760_1_2_12; -.
DR InParanoid; Q8F4I0; -.
DR OMA; TRFCVVS; -.
DR BRENDA; 2.3.1.31; 2986.
DR SABIO-RK; Q8F4I0; -.
DR UniPathway; UPA00051; UER00074.
DR EvolutionaryTrace; Q8F4I0; -.
DR Proteomes; UP000001408; Chromosome I.
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 Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..366
FT /note="Homoserine O-acetyltransferase"
FT /id="PRO_0000155722"
FT DOMAIN 47..349
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:17927957"
FT ACT_SITE 311
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:17927957"
FT ACT_SITE 344
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:17927957"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 27..39
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2PL5"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:2PL5"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:2PL5"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 127..140
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:2PL5"
FT TURN 247..253
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 316..328
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:2PL5"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:2PL5"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:2PL5"
SQ SEQUENCE 366 AA; 40115 MW; 8AADC3E30E30E3F6 CRC64;
MNETGSIGII ETKYAEFKEL ILNNGSVLSP VVIAYETYGT LSSSKNNAIL ICHALSGDAH
AAGYHSGSDK KPGWWDDYIG PGKSFDTNQY FIICSNVIGG CKGSSGPLSI HPETSTPYGS
RFPFVSIQDM VKAQKLLVES LGIEKLFCVA GGSMGGMQAL EWSIAYPNSL SNCIVMASTA
EHSAMQIAFN EVGRQAILSD PNWKNGLYDE NSPRKGLALA RMVGHITYLS DDKMREKFGR
NPPRGNILST DFAVGSYLIY QGESFVDRFD ANSYIYVTKA LDHYSLGKGK ELTAALSNAT
CRFLVVSYSS DWLYPPAQSR EIVKSLEAAD KRVFYVELQS GEGHDSFLLK NPKQIEILKG
FLENPN
