(data stored in ACNUC7421 zone)

SWISSPROT: METXS_PARXL

ID   METXS_PARXL             Reviewed;         381 AA.
AC   Q146X7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JAN-2019, entry version 78.
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=Bxeno_A0074; ORFNames=Bxe_A4388;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-
CC       homoserine, forming succinyl-L-homoserine. {ECO:0000255|HAMAP-
CC       Rule:MF_00296}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + succinyl-CoA = CoA + O-succinyl-L-
CC         homoserine; Xref=Rhea:RHEA:22008, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57476, ChEBI:CHEBI:57661;
CC         EC=2.3.1.46; Evidence={ECO:0000255|HAMAP-Rule:MF_00296};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo 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}.
DR   EMBL; CP000270; ABE28612.1; -; Genomic_DNA.
DR   RefSeq; WP_011486468.1; NZ_CP008760.1.
DR   SMR; Q146X7; -.
DR   STRING; 266265.Bxe_A4388; -.
DR   ESTHER; burxl-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ABE28612; ABE28612; Bxe_A4388.
DR   GeneID; 4005517; -.
DR   KEGG; bxb:DR64_2064; -.
DR   KEGG; bxe:Bxe_A4388; -.
DR   PATRIC; fig|266265.5.peg.75; -.
DR   eggNOG; ENOG4105DWV; Bacteria.
DR   eggNOG; COG2021; LUCA.
DR   HOGENOM; HOG000246301; -.
DR   KO; K00641; -.
DR   OMA; CQGTTGP; -.
DR   OrthoDB; 536745at2; -.
DR   BioCyc; BXEN266265:BXE_RS00365-MONOMER; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000001817; 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; 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;
DR   PRODOM; Q146X7.
DR   SWISS-2DPAGE; Q146X7.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Methionine biosynthesis; Reference proteome; Transferase.
FT   CHAIN         1    381       Homoserine O-succinyltransferase.
FT                                /FTId=PRO_1000021877.
FT   DOMAIN       45    360       AB hydrolase-1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   ACT_SITE    151    151       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   ACT_SITE    321    321       {ECO:0000255|HAMAP-Rule:MF_00296}.
FT   ACT_SITE    354    354       {ECO:0000255|HAMAP-Rule:MF_00296}.
FT   BINDING     221    221       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   BINDING     355    355       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   SITE        323    323       Important for acyl-CoA specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00296}.
SQ   SEQUENCE   381 AA;  42037 MW;  B2C1D91C69ADDBB8 CRC64;
     MESIGIVAPQ KMHFTEPLPL QNGSSLAGYD LMVETYGTLN AARSNAVLVC HALNASHHVA
     GVYADNPRDI GWWDNMVGPG KPLDTDKFFV IGVNNLGSCF GSTGPMSIDP STGNPYGATF
     PVVTVEDWVN AQARVADQFG ITRFAAVMGG SLGGMQALAW SMMYPERVAH CIVVASTPKL
     SAQNIAFNEV ARSAILSDPD FHGGNYYAHN VKPKRGLRVA RMIGHITYLS DDDMAEKFGR
     SLRRAEGALD AYNFNFDVEF EVESYLRYQG DKFADYFDAN TYLLITRALD YFDPAKAFAG
     DLTAAVAHTT AKYLIASFTT DWRFAPARSR ELVKALLDHK RTVTYAEIDA PHGHDAFLLD
     DARYHNLMRA YYERIANEVN A
//

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