METXS_ACIAD
ID METXS_ACIAD Reviewed; 387 AA.
AC Q6FEQ3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:28581482};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
DE Short=HTS {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000305};
GN Name=metXS {ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000303|PubMed:28581482};
GN OrderedLocusNames=ACIAD0529;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF ARG-323.
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:28581482}.
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:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000269|PubMed:28581482};
CC -!- ACTIVITY REGULATION: Requires MetW for activity.
CC {ECO:0000269|PubMed:28581482}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=484 uM for L-homoserine {ECO:0000269|PubMed:28581482};
CC KM=625 uM for succinyl-CoA {ECO:0000269|PubMed:28581482};
CC Note=kcat is 3.42 sec(-1). {ECO:0000269|PubMed:28581482};
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:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; CR543861; CAG67455.1; -; Genomic_DNA.
DR RefSeq; WP_004920083.1; NC_005966.1.
DR AlphaFoldDB; Q6FEQ3; -.
DR SMR; Q6FEQ3; -.
DR STRING; 62977.ACIAD0529; -.
DR ESTHER; aciad-q6feq3; Homoserine_transacetylase.
DR EnsemblBacteria; CAG67455; CAG67455; ACIAD0529.
DR GeneID; 45233008; -.
DR KEGG; aci:ACIAD0529; -.
DR eggNOG; COG2021; Bacteria.
DR HOGENOM; CLU_028760_1_0_6; -.
DR OMA; TRFCVVS; -.
DR OrthoDB; 536745at2; -.
DR BioCyc; ASP62977:ACIAD_RS02400-MON; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000000430; 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; 3.40.50.1820; -; 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 PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..387
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000155702"
FT DOMAIN 49..358
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 321
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 354
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 355
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 323
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
FT MUTAGEN 323
FT /note="R->L: Can no longer use succinyl-CoA as acyl donor,
FT but can use acetyl-CoA."
FT /evidence="ECO:0000269|PubMed:28581482"
SQ SEQUENCE 387 AA; 43671 MW; 3BB57FA2B752040E CRC64;
MSFPSDSVGL VTPQKFQFEE PLHLECGRVL PRFELMVETY GTLNADYSNA ILICHALSGH
HHAAGYHHDD DKKAGWWDAC IGPGKAIDTN KFFVVALNNI GGCNGSTGPT SPNPENENRP
YGPDFPLVTV RDWVKTQALL SDHLGIQSWY AVIGGSLGGM QALQWSVDYP DRLKNCVIIA
SAPKLSAQNI AFNEVARQSI LSDPDFYHGR YLEHDSYPKR GLILARMVGH ITYLSEEAMK
QKFGRDLKSG KFMYGFDVEF QVESYLRYQG EQFSRNFDAN TYLIMTKALD YFDPSREYEQ
SLTKAMAQTQ CRFLVVSFTT DWRFAPERSQ EIVDALITNH KPVTYLDVDA EQGHDSFLFP
IPLYVKTLRA FLGGEAHLKS TPQVEIN
