ID I8T5T6_9GAMM Unreviewed; 382 AA.
AC I8T5T6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=WQQ_26650 {ECO:0000313|EMBL:EIT69083.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT69083.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT69083.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT69083.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIT69083.1}.
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DR EMBL; AKGD01000002; EIT69083.1; -; Genomic_DNA.
DR RefSeq; WP_007185606.1; NZ_AKGD01000002.1.
DR AlphaFoldDB; I8T5T6; -.
DR STRING; 1172194.WQQ_26650; -.
DR PATRIC; fig|1172194.4.peg.2575; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000003704; 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|HAMAP-Rule:MF_00296};
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:UP000003704};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 51..335
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 322
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT ACT_SITE 355
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296,
FT ECO:0000256|PIRSR:PIRSR000443-1"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
FT SITE 324
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00296"
SQ SEQUENCE 382 AA; 42403 MW; 978C5B934C62CF21 CRC64;
MTSEVTEGSV GIVEPRKIRI DSPLILDCGR LFMWHDLMVE TYGTLNAARS NAVLICHALS
GDHHAAGVHS ADDRKPGWWD NCIGPGKPID TDRFFVVSLN NLGGCRGSTG PNSIAPETGR
QWGPDFPLLT VRDWVRSQAL LADKLGITQW AAIVGGSLGG MQVMQWAVDL PRRVRHAVVI
ASAPQISAQN IAFNEIARQA ILSDPDFHGG RYYDHNAVPA RGLRLARMLG HITYLSDAAM
RAKFGNDLKA PQPSFNFDVE FEVESYLRYQ GESFVDRFDA NTYLIMTKAL DYFDPARDYD
DSLVDAFRQA QARFLVVAFS SDWRFSPARS REIVKALVDA GRDVSYALIE SALGHDDFLM
PLPDYHRVLR GYLSRVADEV GA
//
