METXS_RALSO
ID METXS_RALSO Reviewed; 403 AA.
AC Q8Y3F3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00296};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTS {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXS {ECO:0000255|HAMAP-Rule:MF_00296}; OrderedLocusNames=RSc0027;
GN ORFNames=RS01850;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine;
CC Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:57476, ChEBI:CHEBI:57661; EC=2.3.1.46;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00296};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-succinyl-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; AL646052; CAD13555.1; -; Genomic_DNA.
DR RefSeq; WP_010999994.1; NC_003295.1.
DR AlphaFoldDB; Q8Y3F3; -.
DR SMR; Q8Y3F3; -.
DR STRING; 267608.RSc0027; -.
DR ESTHER; ralso-METX; Homoserine_transacetylase.
DR PRIDE; Q8Y3F3; -.
DR DNASU; 1218829; -.
DR EnsemblBacteria; CAD13555; CAD13555; RSc0027.
DR GeneID; 60499536; -.
DR KEGG; rso:RSc0027; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_4; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..403
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000155740"
FT DOMAIN 74..383
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 343
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 376
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 345
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 403 AA; 44506 MW; A42DBAA2895F9880 CRC64;
MTELQVDPAA SADPAAAADT PRHPAATLPP DSVGLVVPER MHFAEPLPLR NGSQLVGYDL
MVETYGTLNA ERSNAVLICH ALNASHHVAG VHAEGEVGWW DNMVGPGKPV DTNRFFVIGV
NNLGSCFGST GPMSPHPQTG QPYGARFPVV TVEDWVNAQA RVADRFGIRQ FAAVMGGSLG
GMQALAWSLM YPERVRHCVV VASTPKLSAQ NIAFNEVARS AILSDPDFHG GDYYAHNVKP
KRGLRVARMI GHITYLSDED MAEKFGRELK AEDIRFSFDV EFQVESYLRY QGDKFAEYFD
ANTYLLITRA LDYFDPALAY EGSLTRAVAH TRASYLVVSF TTDWRFAPAR SRELVKALLD
NKRPVTYGEI DAPHGHDAFL LEDARYHALV RAYYERIAQE IGA
