(data stored in ACNUC7421 zone)

SWISSPROT: METXS_PSEAB

ID   METXS_PSEAB             Reviewed;         379 AA.
AC   Q02U23;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=PA14_05080;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ15356.1; -; Genomic_DNA.
DR   RefSeq; WP_003084535.1; NC_008463.1.
DR   SMR; Q02U23; -.
DR   ESTHER; pseae-metx; Homoserine_transacetylase.
DR   EnsemblBacteria; ABJ15356; ABJ15356; PA14_05080.
DR   KEGG; pau:PA14_05080; -.
DR   HOGENOM; HOG000246301; -.
DR   KO; K00641; -.
DR   OMA; CQGTTGP; -.
DR   BioCyc; PAER208963:G1G74-424-MONOMER; -.
DR   UniPathway; UPA00051; UER00075.
DR   Proteomes; UP000000653; 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;
DR   PRODOM; Q02U23.
DR   SWISS-2DPAGE; Q02U23.
KW   Acyltransferase; Amino-acid biosynthesis; Complete proteome;
KW   Cytoplasm; Methionine biosynthesis; Transferase.
FT   CHAIN         1    379       Homoserine O-succinyltransferase.
FT                                /FTId=PRO_1000021894.
FT   DOMAIN       51    360       AB hydrolase-1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   ACT_SITE    157    157       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   ACT_SITE    323    323       {ECO:0000255|HAMAP-Rule:MF_00296}.
FT   ACT_SITE    356    356       {ECO:0000255|HAMAP-Rule:MF_00296}.
FT   BINDING     227    227       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   BINDING     357    357       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00296}.
FT   SITE        325    325       Important for acyl-CoA specificity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00296}.
SQ   SEQUENCE   379 AA;  41834 MW;  8744551ABF35AF45 CRC64;
     MPTVFPDDSV GLVSPQTLHF NEPLELTSGK SLAEYDLVIE TYGELNATQS NAVLICHALS
     GHHHAAGYHS VDERKPGWWD SCIGPGKPID TRKFFVVALN NLGGCNGSSG PASINPATGK
     VYGADFPMVT VEDWVHSQAR LADRLGIRQW AAVVGGSLGG MQALQWTISY PERVRHCLCI
     ASAPKLSAQN IAFNEVARQA ILSDPEFLGG YFQEQGVIPK RGLKLARMVG HITYLSDDAM
     GAKFGRVLKT EKLNYDLHSV EFQVESYLRY QGEEFSTRFD ANTYLLMTKA LDYFDPAAAH
     GDDLVRTLEG VEADFCLMSF TTDWRFSPAR SREIVDALIA AKKNVSYLEI DAPQGHDAFL
     MPIPRYLQAF SGYMNRISV
//

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