ID A0A0B7J1Z8_9PROT Unreviewed; 375 AA.
AC A0A0B7J1Z8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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:CEN56654.1};
GN Synonyms=metXS {ECO:0000256|HAMAP-Rule:MF_00296};
GN ORFNames=BN1209_1619 {ECO:0000313|EMBL:CEN56654.1};
OS Candidatus Methylopumilus turicensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN56654.1, ECO:0000313|Proteomes:UP000056322};
RN [1] {ECO:0000313|Proteomes:UP000056322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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; LN794158; CEN56654.1; -; Genomic_DNA.
DR RefSeq; WP_045751708.1; NZ_LN794158.1.
DR AlphaFoldDB; A0A0B7J1Z8; -.
DR STRING; 1581680.BN1209_1619; -.
DR KEGG; mbac:BN1209_1619; -.
DR HOGENOM; CLU_028760_1_2_4; -.
DR OrthoDB; 9800754at2; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000056322; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000056322};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00296}.
FT DOMAIN 48..355
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; 41486 MW; CE1EC4F55787DF53 CRC64;
MSENSSVGIV APQIAHFNSP LTLKSGQVLP QFNLMYETYG ELNADKSNAV LICHALSGHH
HVAGKHHEDD KNPGWWDNLI GPGKPLDTNK FFVIGLNNLG GCHGSSGPLS TNPDTDRPWG
ASFPILTVED WVNSQARLAD FLGIKQLAAV LGGSLGGMQA LQWSIAYPER MRHALVIASA
PNLTAQNIAF NEVARQAIIT DPEFYEGDYY NHGAVPRRGL RIARMLGHIT YLSDDAMGAK
FGRKLRDGNI KYGFDVEFEM ESYLRYQGDK FAGEFDANTY LRMTRALDYF DPAFEHGGDL
SAALAKVTAD FLVVSFTSDW RFSPARSREI VKALLDNELS VSYAEVTAAH GHDAFLMPDA
HYHNIMRAYF AKIEV
//
