ID A0A1U6GJQ5_9GAMM Unreviewed; 475 AA.
AC A0A1U6GJQ5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000256|HAMAP-Rule:MF_00296};
DE Short=HST {ECO:0000256|HAMAP-Rule:MF_00296};
DE EC=2.3.1.46 {ECO:0000256|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000256|HAMAP-Rule:MF_00296};
DE Short=HTS {ECO:0000256|HAMAP-Rule:MF_00296};
GN Name=metX {ECO:0000313|EMBL:SLJ83690.1};
GN Synonyms=metXS {ECO:0000256|HAMAP-Rule:MF_00296};
GN ORFNames=DABAL43B_0476 {ECO:0000313|EMBL:SLJ83690.1};
OS Psychrobacter sp. DAB_AL43B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1028416 {ECO:0000313|EMBL:SLJ83690.1, ECO:0000313|Proteomes:UP000190084};
RN [1] {ECO:0000313|EMBL:SLJ83690.1, ECO:0000313|Proteomes:UP000190084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAB_AL43B {ECO:0000313|EMBL:SLJ83690.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000256|HAMAP-Rule:MF_00296}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00296}.
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DR EMBL; LT799838; SLJ83690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U6GJQ5; -.
DR STRING; 1028416.DABAL43B_0476; -.
DR KEGG; psyc:DABAL43B_0476; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000190084; Chromosome i.
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; alpha/beta hydrolase; 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 NCBIfam; TIGR01392; homoserO_Ac_trn; 1.
DR PANTHER; PTHR32268; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR32268:SF11; HOMOSERINE O-ACETYLTRANSFERASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00296,
KW ECO:0000313|EMBL:SLJ83690.1};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 79..403
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 395
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT SITE 397
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 475 AA; 52555 MW; 9E2DCD9F08AD431B CRC64;
MNARPDNTSD QFSKEKPHSV SSVNDADSVS SVGPVGSVGI VTPQTFHFAE PLTLECNRTL
PSFDLIVETY GTLNSAKSNA VLICHALSGS HHAAGFHSAD DKKSGWWDNM IGPNKAIDTN
RFFVVCVNNI GSCFGSTGPT TINPDSTADG DEGRAYGPDF PLVTIKDWVK TQAMLSDRLG
IDVWHAIVGG SMGGMQAMQW AVDYPDRLKR CVVIACTPKL SAQNIAFNEV ARQSILSDPD
FKEGRYLQAG TYPRRGLILA RMVGHITYLT DDAMKAKFGR DLKSGKFMYG YDVEFQVESY
LRYQGERFSE NFDANTYLLM TKALDYFDPT RDYPLTSSNS DSVKVDSSEN EIAETLAGST
DIDNMSENNH QELTALKAAF AHTQCQYLIV SFTTDWRFAP ERSQEIVDAL MATGKPVSYI
NIDAPHGHDS FLFDIPRYMG AVRGFLTAPF MTDNQVENNR QKNHQSSHQK AGERS
//
