ID   METXS_MAGMM             Reviewed;         394 AA.
AC   A0LCI7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Mmc1_3190;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK45680.1; -; Genomic_DNA.
DR   RefSeq; WP_011714743.1; NC_008576.1.
DR   AlphaFoldDB; A0LCI7; -.
DR   SMR; A0LCI7; -.
DR   STRING; 156889.Mmc1_3190; -.
DR   ESTHER; magsm-metx; Homoserine_transacetylase.
DR   PRIDE; A0LCI7; -.
DR   EnsemblBacteria; ABK45680; ABK45680; Mmc1_3190.
DR   KEGG; mgm:Mmc1_3190; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_1_2_5; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000002586; 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; Reference proteome; Transferase.
FT   CHAIN           1..394
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_1000119458"
FT   DOMAIN          54..368
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        160
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         365
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            333
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   394 AA;  43454 MW;  3EF9D147C0D680A0 CRC64;
     MTHEPLTASV GIVTPQHVRL FGASTPLQLD GGTLLHSVDV SYETYGTLNQ ERSNAVLICH
     ALSGNAHAAG YHSKDDKRPG WWDHYIGPGK PFDTNRYFVI ASNNLGGCDG TTGPSSIDPA
     TGMPYGLNFP MITIGDIVRV QHALVRQLGI ERLMAVVGGS MGGMQALQWA LDYPHMVPAS
     VIIAAAPRLT AQNIAFNAVA RQAIMADPHF NGGDYYTLPG DPTTKARPES GLALARMMAH
     ITYLSEQGLH ERFGRRLQDR DALSYGFETD FAVESYLSYQ GSSFVKRFDA NSYLYITKAM
     DYFDPFPDAE TTVQRLTGVE SHFLVMSFDT DWRFDTSRSK ELVRILHRSL KDCTFQEFSS
     PAGHDAFLLP HPSYEKSLGS FLLRTWQSIT GGQA