ID   METXS_PSYA2             Reviewed;         445 AA.
AC   Q4FUR4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=Psyc_0375;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ18244.1; -; Genomic_DNA.
DR   RefSeq; WP_011279682.1; NC_007204.1.
DR   AlphaFoldDB; Q4FUR4; -.
DR   SMR; Q4FUR4; -.
DR   STRING; 259536.Psyc_0375; -.
DR   ESTHER; psyar-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; AAZ18244; AAZ18244; Psyc_0375.
DR   KEGG; par:Psyc_0375; -.
DR   eggNOG; COG2021; Bacteria.
DR   HOGENOM; CLU_028760_7_0_6; -.
DR   OMA; TRFCVVS; -.
DR   OrthoDB; 536745at2; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000000546; 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; -; 2.
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..445
FT                   /note="Homoserine O-succinyltransferase"
FT                   /id="PRO_0000231884"
FT   DOMAIN          45..411
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   ACT_SITE        406
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   BINDING         407
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT   SITE            375
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   445 AA;  49314 MW;  110C21B942B9BC1E CRC64;
     MNSVGVVKPQ TLHFAEPLTL ECNRTLPSFE LIIETYGTLN SDKSNAVLIC HALSGSHHAA
     GFHSDNDKKA GWWDNMIGPN KSIDTNRFFV VCVNNIGSCF GSTGPTSINP ESSKAQVYGP
     DFPLVTIKDW VKTQAMLSDR LEIDVWHAVV GGSMGGMQAL QWAADYPSRL KRCVVIASTP
     KLSAQNIAFN EVARQSILSD PDFKNGRYLQ AGTYPRRGLI LARMVGHITY LTDDAMKAKF
     GRDLKSGKFM YGYDVEFQVE SYLRYQGERF SENFDANTYL LMTKALDYFD PTRDYPLTQS
     AQPIDSLVPE ELLASSLVES VKADSSEDEL AKTLADSADI DNISASNHQE LTALKAAFAH
     TECQYLIVSF TTDWRFAPER SQEIVDALMA TGKPVSYINV DAPHGHDSFL FDIPRYMGAV
     KGFLNAPFMT DNQSKNSQQK LGARS