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Database: UniProt
Entry: A0A1H8D7V2_9PROT
LinkDB: A0A1H8D7V2_9PROT
Original site: A0A1H8D7V2_9PROT 
ID   A0A1H8D7V2_9PROT        Unreviewed;       375 AA.
AC   A0A1H8D7V2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05216325_106102 {ECO:0000313|EMBL:SEN03401.1};
OS   Nitrosomonas marina.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=917 {ECO:0000313|EMBL:SEN03401.1, ECO:0000313|Proteomes:UP000199459};
RN   [1] {ECO:0000313|EMBL:SEN03401.1, ECO:0000313|Proteomes:UP000199459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nm22 {ECO:0000313|EMBL:SEN03401.1,
RC   ECO:0000313|Proteomes:UP000199459};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOCP01000006; SEN03401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8D7V2; -.
DR   STRING; 917.SAMN05216326_1167; -.
DR   OrthoDB; 9800754at2; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000199459; Unassembled WGS sequence.
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|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_00296}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00296};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW   Rule:MF_00296};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00296}.
FT   DOMAIN          48..356
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        319
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT                   ECO:0000256|PIRSR:PIRSR000443-1"
FT   ACT_SITE        352
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         353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT   SITE            321
FT                   /note="Important for acyl-CoA specificity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ   SEQUENCE   375 AA;  41799 MW;  1C4D167C0390A00F CRC64;
     MPESNSVGIV TPQYVHIDKP LELKSGTVIS SYNLVYETYG TLNAERSNAV LVCHALSGNH
     HVAGVYEDKP KSTGWWDNMV GPGKPIDTDK FFVIGMNNLG GCHGSTGPAS IDARTGKHYG
     ANFPIVTVED WVETQAQLAE HLGIHQFAAV VGGSLGGMQA LQWTLDYPDK VRHALVIAAA
     AKLTAQNIAF NDVARQAILT DQDYYGGDYY SYNTLPRRGL RLARMLGHIT YLSDHSMASK
     FGRELRDGKF SFGYDVEFEI ESYLRYQGDK FTDLFDANSY LLMTKALDYF DPANAYNGDL
     IAAFKAARAS FLVLSFTTDW RFSPERSRDI VEALLDNNIN VSYGEITSTH GHDSFLMNDA
     YYHQLVRTYM KNIEV
//
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