ID   METXS_NEIMA             Reviewed;         379 AA.
AC   Q9JUT9; A1IRF6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
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}; OrderedLocusNames=NMA1136;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08342.1; -; Genomic_DNA.
DR   PIR; C81880; C81880.
DR   RefSeq; WP_002246134.1; NC_003116.1.
DR   AlphaFoldDB; Q9JUT9; -.
DR   SMR; Q9JUT9; -.
DR   ESTHER; neima-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; CAM08342; CAM08342; NMA1136.
DR   KEGG; nma:NMA1136; -.
DR   HOGENOM; CLU_028760_1_2_4; -.
DR   OMA; TRFCVVS; -.
DR   BioCyc; NMEN122587:NMA_RS05705-MON; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000000626; 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_0000155732"
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"
SQ   SEQUENCE   379 AA;  42109 MW;  CC15CC922286F724 CRC64;
     MSQNASVGIV TPQKIPFEMP LVLENGKTLP RFDLMIETYG ELNAEKNNAV LICHALSGNH
     HVAGRHSAED KYTGWWDNMV GPGKPIDTER FFVVGLNNLG GCDGSSGPLS INPETGREYG
     ADFPVVTVKD WVKSQAALTD YLGIGQWAAV VGGSLGGMQA LQWTISYPER VRHALVIASA
     PKLSTQNIAF NDVARQAILT DPDFNEGHYR SRNTVPARGL RIARMMGHIT YLAEDGLGKK
     FGRDLRSNGY QYGYGVEFEV ESYLRYQGDK FVGRFDANTY LLMTKALDYF DPAADFGNSL
     TRAVQDVQAK FFVASFSTDW RFAPERSHEL VKALIAAQKS VQYIEVKSAH GHDAFLMEDE
     AYMRAVAAYM NNVYKECQQ