METXS_PSEPG
ID METXS_PSEPG Reviewed; 379 AA.
AC B0KN51;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=PputGB1_5147;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABZ01032.1; -; Genomic_DNA.
DR RefSeq; WP_012274649.1; NC_010322.1.
DR AlphaFoldDB; B0KN51; -.
DR SMR; B0KN51; -.
DR STRING; 76869.PputGB1_5147; -.
DR ESTHER; psepu-METX; Homoserine_transacetylase.
DR EnsemblBacteria; ABZ01032; ABZ01032; PputGB1_5147.
DR KEGG; ppg:PputGB1_5147; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000002157; 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; Transferase.
FT CHAIN 1..379
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_1000078946"
FT DOMAIN 51..360
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 323
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 356
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 325
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ SEQUENCE 379 AA; 41590 MW; 6456712FAA9F5F45 CRC64;
MSTVFPVDSV GLVVPQTARF DEPLALACGR SLASYELVYE TYGTLNASAS NAVLICHALS
GHHHAAGYHA ATDRKPGWWD SCIGPGKPID TNRFFVVSLN NLGGCNGSTG PSSVNPATGK
PYGADFPVLT VEDWVHSQVR LGERLGIQQW AAVVGGSLGG MQALQWTISY PERVRHCVDI
ASAPKLSAQN IAFNEVARQA ILTDPEFHGG SFQDQGVIPK RGLMLARMVG HITYLSDDSM
GEKFGRELKS DKLNYDFHSV EFQVESYLRY QGEEFSGRFD ANTYLLMTKA LDYFDPAAAQ
GGDLAATLAH VTADYCIMSF TTDWRFSPAR SREIVDALMA ARKNVCYLEI DSPYGHDAFL
IPTPRYMQGF SNYMNRIAI
