METXS_COMTK
ID METXS_COMTK Reviewed; 409 AA.
AC B7X2B6;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=CtesDRAFT_PD5178 {ECO:0000312|EMBL:EED70230.1};
OS Comamonas testosteroni (strain DSM 14576 / KF-1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=399795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14576 / KF-1;
RX PubMed=15240283; DOI=10.1128/aem.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
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; AAUJ02000001; EED70230.1; -; Genomic_DNA.
DR RefSeq; WP_003060196.1; NZ_AAUJ02000001.1.
DR AlphaFoldDB; B7X2B6; -.
DR SMR; B7X2B6; -.
DR STRING; 399795.CtesDRAFT_PD5178; -.
DR EnsemblBacteria; EED70230; EED70230; CtesDRAFT_PD5178.
DR eggNOG; COG2021; Bacteria.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000003039; Unassembled WGS sequence.
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; Transferase.
FT CHAIN 1..409
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000440301"
FT DOMAIN 43..380
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT REGION 244..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 341
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 374
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 343
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
SQ SEQUENCE 409 AA; 45041 MW; 0BFCC48D0A33EA4D CRC64;
MSFIATPQFM HFDEPLPLQS GGSIADYDLA FETYGQLNAD KSNAIVVCHA LNASHHVAGS
YEGQPKSEGW WDNMIGPGKP VDTDKFFVIG INNLGSCFGS TGPMHTNPAT GKPYGADFPV
VTVEDWVDAQ ARLLDRLGIQ TLAAVLGGSL GGMQALSWSL RYPERMRHAV VVASAPNLNA
ENIAFNEVAR RAIVTDPDFN GGHFYEHGVV PARGLRIARM VGHITYLSDD VMNQKFGRSL
RAPTLPAARG SLPPEGTDPT RGGPASDRRD YLYSTQDVEF QIESYLRYQG EKFSGYFDAN
TYLLITRALD YFDPARCHDG DLTRALAVAK ARFLLVSFTT DWRFAPARSR EIVKSLLENN
RDVSYAEIDA PHGHDAFLLD DPRYMSVMRS YFEGIAKELK TTERAGGAA
