ID Q9Z3X6_9RALS Unreviewed; 345 AA.
AC Q9Z3X6;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase {ECO:0000256|ARBA:ARBA00035695};
DE EC=4.1.2.45 {ECO:0000256|ARBA:ARBA00035679};
DE AltName: Full=2'-hydroxybenzalpyruvate aldolase {ECO:0000256|ARBA:ARBA00035718};
GN Name=nagE {ECO:0000313|EMBL:AAD12616.1};
OS Ralstonia sp. U2.
OG Plasmid pWWU2 {ECO:0000313|EMBL:AAD12616.1}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=70356 {ECO:0000313|EMBL:AAD12616.1};
RN [1] {ECO:0000313|EMBL:AAD12616.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U2 {ECO:0000313|EMBL:AAD12616.1};
RC PLASMID=pWWU2 {ECO:0000313|EMBL:AAD12616.1};
RX PubMed=9573207;
RA Fuenmayor S.L., Wild M., Boyes A.L., Williams P.A.;
RT "A gene cluster encoding steps in conversion of naphthalene to gentisate in
RT Pseudomonas sp. strain U2.";
RL J. Bacteriol. 180:2522-2530(1998).
RN [2] {ECO:0000313|EMBL:AAD12616.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U2 {ECO:0000313|EMBL:AAD12616.1};
RC PLASMID=pWWU2 {ECO:0000313|EMBL:AAD12616.1};
RA Fuenmayor S., Wild M., Boyes A.L., Williams P.A.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AAD12616.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=U2 {ECO:0000313|EMBL:AAD12616.1};
RC PLASMID=pWWU2 {ECO:0000313|EMBL:AAD12616.1};
RX PubMed=11133965; DOI=10.1128/JB.183.2.700-708.2001;
RA Zhou N.Y., Fuenmayor S.L., Williams P.A.;
RT "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding
RT enzymes for gentisate catabolism.";
RL J. Bacteriol. 183:700-708(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3E)-4-(2-hydroxyphenyl)-2-oxobut-3-enoate + H2O = pyruvate +
CC salicylaldehyde; Xref=Rhea:RHEA:27389, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16008, ChEBI:CHEBI:59353; EC=4.1.2.45;
CC Evidence={ECO:0000256|ARBA:ARBA00035599};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000256|ARBA:ARBA00035632}.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF036940; AAD12616.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9Z3X6; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00952; CHBPH_aldolase; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR048038; HBPHA/CBPHA.
DR PANTHER; PTHR12128:SF51; BLL4205 PROTEIN; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Plasmid {ECO:0000313|EMBL:AAD12616.1};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:AAD12616.1}.
SQ SEQUENCE 345 AA; 38181 MW; 44632D707BB51B81 CRC64;
MTRKTSKAVR LTAADIQGAW VIMPTPSTPD ASDWRSTHTV DLDETARIVE ELIAAGVNGI
LSHGTFGECA TLTWEEKRDF VSTVVETARG RVPYFCGTTA LNTREVIRQT RELIDIGAQG
TMLGVPMWVK MDLPTAVQFY RDVAEAVPDA AIAVYANPEA FKFDFPRPFW AEMSKIPQVV
TAKYLGIGML DLDLKLAPNI RFLPHEDDYY AAARINPERM TAFWSSGSMC GPATALVLRD
EVVKAKNTGD WAKAKAISDD MRAADATLFP RGDFSEFSKY NIGLEKARMD EAGWLKAGPC
RPPYTLVPDE YLAGARKSGK AWAALHTKYA KELRKTKTAT NSKKK
//
