METXS_BORPD
ID METXS_BORPD Reviewed; 424 AA.
AC A9I0E6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
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, ECO:0000303|PubMed:28581482};
GN OrderedLocusNames=Bpet0417;
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. In vitro, has also serine succinyl
CC transferase activity. {ECO:0000269|PubMed:28581482}.
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 ECO:0000269|PubMed:28581482};
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; AM902716; CAP40749.1; -; Genomic_DNA.
DR AlphaFoldDB; A9I0E6; -.
DR SMR; A9I0E6; -.
DR STRING; 94624.Bpet0417; -.
DR ESTHER; borpd-metx; Homoserine_transacetylase.
DR EnsemblBacteria; CAP40749; CAP40749; Bpet0417.
DR KEGG; bpt:Bpet0417; -.
DR eggNOG; COG2021; Bacteria.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000001225; 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 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..424
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_1000115211"
FT DOMAIN 67..381
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 342
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 375
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 344
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 424 AA; 45530 MW; BA5DCF531303AF9F CRC64;
MTTPVPVPNG GPAPAAVPAA AEPGSVGIVT PQLIRFDTPL PLASGQSLQS YELAVETYGT
LNAGRTNAVL VCHALNASHH VAGLAADDPN DVGWWDNMVG PGKPLDTNRF FVIGVNNLGS
CFGSTGPASI NPATGHPWGA AFPVLTVEDW VHAQARLADH FGIERFAAVM GGSLGGMQAL
SWAITCPERV AHCIVIASTP RLSAQNIGFN EVARRAIITD PDFHGGDYYA HNTVPRRGLS
VARMIGHITY LSDDDMAEKF GRTQREPAEG GAYRYGYDVE FEVESYLRYQ GEKFSRYFDA
NTYLLITRAL DYFDPARGTG GDLARALKPA QADFLLVSFS TDWRFPPERS REIVRALLKN
GSPVTYAEID APHGHDAFLL DDARYHAVVR GYYERIAREL GLDEPAAGAA PAAAEPACAE
GCAA
