METXS_PSEAE
ID METXS_PSEAE Reviewed; 379 AA.
AC P57714; Q9I6A5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=PA0390;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROBABLE FUNCTION AS A SUCCINYLTRANSFERASE, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7704274; DOI=10.1099/13500872-141-2-431;
RA Foglino M., Borne F., Bally M., Ball G., Patte J.-C.;
RT "A direct sulfhydrylation pathway is used for methionine biosynthesis in
RT Pseudomonas aeruginosa.";
RL Microbiology 141:431-439(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
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, ECO:0000305|PubMed:7704274}.
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 -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
CC {ECO:0000250|UniProtKB:P07623, ECO:0000255|HAMAP-Rule:MF_00296,
CC ECO:0000305|PubMed:7704274}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
CC -!- DISRUPTION PHENOTYPE: Methionine auxotroph. Defect is complemented by
CC expression of the E.coli metA gene. {ECO:0000269|PubMed:7704274}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000255|HAMAP-Rule:MF_00296}.
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DR EMBL; AE004091; AAG03779.1; -; Genomic_DNA.
DR PIR; E83597; E83597.
DR RefSeq; NP_249081.1; NC_002516.2.
DR RefSeq; WP_003084535.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; P57714; -.
DR SMR; P57714; -.
DR STRING; 287.DR97_3357; -.
DR ESTHER; pseae-metx; Homoserine_transacetylase.
DR PaxDb; P57714; -.
DR PRIDE; P57714; -.
DR DNASU; 878549; -.
DR EnsemblBacteria; AAG03779; AAG03779; PA0390.
DR GeneID; 878549; -.
DR KEGG; pae:PA0390; -.
DR PATRIC; fig|208964.12.peg.410; -.
DR PseudoCAP; PA0390; -.
DR HOGENOM; CLU_028760_1_2_6; -.
DR InParanoid; P57714; -.
DR OMA; TRFCVVS; -.
DR PhylomeDB; P57714; -.
DR BioCyc; PAER208964:G1FZ6-394-MON; -.
DR UniPathway; UPA00051; UER00075.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0008899; F:homoserine O-succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009092; P:homoserine metabolic process; IBA:GO_Central.
DR GO; GO:0009086; P:methionine biosynthetic process; IBA:GO_Central.
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..379
FT /note="Homoserine O-succinyltransferase"
FT /id="PRO_0000155737"
FT DOMAIN 51..360
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 157
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 323
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT ACT_SITE 356
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT BINDING 357
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296"
FT SITE 325
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00296,
FT ECO:0000305|PubMed:28581482"
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
