METXS_BREDA
ID METXS_BREDA Reviewed; 369 AA.
AC F4QV02;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
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 ORFNames=BDIM_02360 {ECO:0000312|EMBL:EGF96431.1};
OS Brevundimonas diminuta (strain ATCC 11568 / DSM 7234 / NBRC 12697 / NCIMB
OS 9393 / NCTC 8545).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=751586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11568 / DSM 7234 / JCM 2788/ NBRC 12697 / NCIMB 9393 / NCTC
RC 8545;
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00296,
CC 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; GL883084; EGF96431.1; -; Genomic_DNA.
DR RefSeq; WP_003163757.1; NZ_GL883084.1.
DR AlphaFoldDB; F4QV02; -.
DR SMR; F4QV02; -.
DR GeneID; 56578021; -.
DR HOGENOM; CLU_028760_3_0_5; -.
DR OrthoDB; 536745at2; -.
DR UniPathway; UPA00051; UER00075.
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.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..369
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000440300"
FT DOMAIN 107..353
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 90..93
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 316
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 346
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 176
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
FT SITE 212
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 369 AA; 40517 MW; 57418A35DFEFC122 CRC64;
MTLALISTET TEEPSCKASV AAPAPKGGAQ IGVKAARRPS ELLQRDGAHD VAVAIPDDFE
LDFGGTLTQK RVIGRLHGKA NAPLIVVAGG ISADRYVHRT ETKGLGWWSG AVGVRAPIDL
TRFRVLAFDF APEFGEDVKD AKTPLTITTQ DQARLLALLL DHLGVEKVAA FIGCSYGGMI
ALAFGELFPD WAEQLVVVSA AHRPHPLATA WRGIQRRILQ LGLETGRIDQ AVGLARELAM
TTYRTQEEFG DRFDSEAPSH AGQAYPVCDY LQARGRAYRD RTTPSRWLSL SDSIDRHRVE
PEAITAPVTL IGFTTDRLCP IEDMRELADR LPNLWRFEQH ASVYGHDAFL KEDKLVADIL
TSVLKDIDQ
