METXS_ACIB3
ID METXS_ACIB3 Reviewed; 386 AA.
AC B7H098;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Homoserine O-succinyltransferase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HST {ECO:0000255|HAMAP-Rule:MF_00296};
DE EC=2.3.1.46 {ECO:0000255|HAMAP-Rule:MF_00296};
DE AltName: Full=Homoserine transsuccinylase {ECO:0000255|HAMAP-Rule:MF_00296};
DE Short=HTS {ECO:0000255|HAMAP-Rule:MF_00296};
GN Name=metXS {ECO:0000255|HAMAP-Rule:MF_00296};
GN OrderedLocusNames=ABBFA_003062;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(2008).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine,
CC forming succinyl-L-homoserine. {ECO:0000255|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:0000255|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: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; CP001172; ACJ59159.1; -; Genomic_DNA.
DR RefSeq; WP_000009638.1; NZ_CP001172.1.
DR AlphaFoldDB; B7H098; -.
DR SMR; B7H098; -.
DR ESTHER; acib3-metx; Homoserine_transacetylase.
DR HOGENOM; CLU_028760_1_2_6; -.
DR OMA; TRFCVVS; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000006924; 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 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Transferase.
FT CHAIN 1..386
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_1000119455"
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"
SQ SEQUENCE 386 AA; 43322 MW; 62FA65C26A0BE683 CRC64;
MSFPADSVGL VTPQKFQFEE PLHLECGRVL PRFELMVETY GTLNADKSNA ILICHALSGH
HHAAGYHHED DKKAGWWDSC IGPGKAIDTN KFFVVALNNI GGCSGSTGPT SPNPENDNRP
YGPDFPLVTV RDWVKTQAML SDRLGISVWY AVVGGSLGGM QALQWSVDYP DRLQKCVVIA
SAPKLSAQNI AFNEVARQSI LSDPDFHHGR YLEKDSYPKR GLILARMVGH ITYLSEEAMK
QKFGRDLKSG KFMYGFDVEF QVESYLRYQG EQFSRNFDAN TYLIMTKALD YFDPSREYGH
SLTEAMSKTK CQFLIVSFTT DWRFAPSRSQ EIVDALITNQ KPVSYLDIDA EQGHDSFLFP
IPLYVKTLRA FLGGEEHLKS TSLEAS