ID F3L3I5_9GAMM Unreviewed; 380 AA.
AC F3L3I5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=metXS {ECO:0000256|HAMAP-Rule:MF_00296};
GN ORFNames=EYZ66_13505 {ECO:0000313|EMBL:QHJ89254.1}, IMCC3088_2177
GN {ECO:0000313|EMBL:EGG29097.1};
OS Aequoribacter fuscus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Aequoribacter.
OX NCBI_TaxID=2518989 {ECO:0000313|EMBL:EGG29097.1, ECO:0000313|Proteomes:UP000005615};
RN [1] {ECO:0000313|EMBL:EGG29097.1, ECO:0000313|Proteomes:UP000005615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:EGG29097.1,
RC ECO:0000313|Proteomes:UP000005615};
RX PubMed=21551310; DOI=10.1128/JB.05111-11;
RA Jang Y., Oh H.M., Kang I., Lee K., Yang S.J., Cho J.C.;
RT "Genome sequence of strain IMCC3088, a proteorhodopsin-containing marine
RT bacterium belonging to the OM60/NOR5 clade.";
RL J. Bacteriol. 193:3415-3416(2011).
RN [2] {ECO:0000313|EMBL:QHJ89254.1, ECO:0000313|Proteomes:UP000464557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC3088 {ECO:0000313|EMBL:QHJ89254.1,
RC ECO:0000313|Proteomes:UP000464557};
RA Li S.-H.;
RT "Halieaceae_genomes.";
RL Submitted (FEB-2019) 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; AEIG01000064; EGG29097.1; -; Genomic_DNA.
DR EMBL; CP036423; QHJ89254.1; -; Genomic_DNA.
DR RefSeq; WP_009576354.1; NZ_CP036423.1.
DR AlphaFoldDB; F3L3I5; -.
DR STRING; 2518989.IMCC3088_2177; -.
DR KEGG; afus:EYZ66_13505; -.
DR eggNOG; COG2021; Bacteria.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000005615; Unassembled WGS sequence.
DR Proteomes; UP000464557; 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; 1.10.1740.110; -; 1.
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:QHJ89254.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000005615};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 48..357
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 321
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 354
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT SITE 323
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 380 AA; 41826 MW; DBD42251FFE259BF CRC64;
MSEHNSVGIV SPQTAHFDAP LALACGKTLN EFDLVYETYG ELNAEKTNAI LICHALSGHH
HAAGYHSESE TKPGWWDTCI GPGKPIDTNV YFVVSLNNLG GCHGSTGPTS INPETGKLWG
PDFPQVRVAD WVNSQAALAD RLGIDIWAAV IGGSLGGMQA MQWSVQYPER LKYCLIIASA
MDLSAQNIAF NEIARQAIQS DPNFCAGHYR EQDTNPSQGL ALARMVGHVT YLSDDAMANK
FGRDIRSGSI EHNIDQEVEF QVESYLRYQG SQFSTAFDAN TYILMTRALD YFDIAADFNG
DPVKAFATTK AQFLVVSFST DWRFSPRRSR EITNALIAAN RPVSYAEIEA AEGHDAFLMP
IPRYLDVLKA YLGRIAEDLL
//
