ID   METXS_NEIGO             Reviewed;         379 AA.
AC   A0A0I9QGZ7;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2015, sequence version 1.
DT   03-AUG-2022, entry version 30.
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};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   ACTIVITY REGULATION.
RC   STRAIN=DSM 9188;
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   -!- ACTIVITY REGULATION: Activity increases in the presence of MetW.
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; LN871225; CTQ31228.1; -; Genomic_DNA.
DR   RefSeq; WP_003699859.1; NZ_UGRA01000001.1.
DR   AlphaFoldDB; A0A0I9QGZ7; -.
DR   SMR; A0A0I9QGZ7; -.
DR   PATRIC; fig|485.41.peg.1815; -.
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.
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..379
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_0000440304"
FT   DOMAIN          48..357
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        154
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        319
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            321
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT                   ECO:0000305|PubMed:28581482"
SQ   SEQUENCE   379 AA;  42147 MW;  8ACB4FE0D2374486 CRC64;
     MSQNTSVGIV TPQKIPFEMP LVLENGKTLP RFDLMIETYG ELNAEKNNAV LICHALSGNH
     HVAGKHSAED KYTGWWDNMV GPGKPIDTER FFVVGLNNLG GCDGSSGPLS INPETGREYG
     ADFPMVTVKD WVKSQAALAD YLGIEQWAAV VGGSLGGMQA LQWAISYPER VRHALVIASA
     PKLSTQNIAF NDVARQAILT DPDFNEGHYR SHNTVPARGL RIARMMGHIT YLAEDGLGKK
     FGRDLRSNGY QYGYSVEFEV ESYLRYQGDK FVGRFDANTY LLMTKALDYF DPAADFGNSL
     TRAVQDVQAK FFVASFSTDW RFAPERSHEL VKALIAAQKS VQYIEVKSAH GHDAFLMEDE
     AYMRAVTAYM NNVDKDCRL