METXS_CUPTR
ID METXS_CUPTR Reviewed; 393 AA.
AC B2AGC8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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};
GN OrderedLocusNames=RALTA_A0154;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAP62827.1; -; Genomic_DNA.
DR RefSeq; WP_012351495.1; NC_010528.1.
DR AlphaFoldDB; B2AGC8; -.
DR SMR; B2AGC8; -.
DR STRING; 977880.RALTA_A0154; -.
DR ESTHER; cuppj-metx; Homoserine_transacetylase.
DR EnsemblBacteria; CAP62827; CAP62827; RALTA_A0154.
DR GeneID; 29760398; -.
DR KEGG; cti:RALTA_A0154; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_4; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR BioCyc; CTAI977880:RALTA_RS00760-MON; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000001692; Chromosome 1.
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; Transferase.
FT CHAIN 1..393
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_1000115222"
FT DOMAIN 62..372
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 168
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 333
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 366
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 335
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 393 AA; 43160 MW; F9C552AEC8534F25 CRC64;
MTDVALPTAA PAAFDLPPDS VGVVAPQRMH FAEPLKLRNG SSIAGYDLMV ETYGTLNADR
SNAVLVCHAL NASHHVAGVY ADDRRNVGWW DNMVGPGKPL DTNRFFVIGI NNLGSCFGST
GPMSLNPATG APYGAAFPVV TVEDWVNAQA RVADAFGITQ FAAVMGGSLG GMQAVAWSLM
YPDRLRHCIV IASTPKLSAQ NIAFNEVARS AILSDPDFHG GNYYAHGVKP KRGLRVARMI
GHITYLSDED MAEKFGRELK SEDIRFSFDV EFQVESYLRY QGDKFAEYFD ANTYLLITRA
LDYFDPALAH GGDLTRAMAQ TQASFLVASF GTDWRFAPSR SRELVKALLD NKRPVSYAEI
DAPHGHDAFL LDDPRYHNLM RAYYDRIAEE IGA
