ID Q1XGL4_PSEPU Unreviewed; 331 AA.
AC Q1XGL4;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, 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=nahE {ECO:0000313|EMBL:BAE92162.1};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid NAH7 {ECO:0000313|EMBL:BAE92162.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303 {ECO:0000313|EMBL:BAE92162.1};
RN [1] {ECO:0000313|EMBL:BAE92162.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G7 {ECO:0000313|EMBL:BAE92162.1};
RC PLASMID=NAH7 {ECO:0000313|EMBL:BAE92162.1};
RX PubMed=2175388; DOI=10.1007/BF00315794;
RA Tsuda M., Iino T.;
RT "Naphthalene degrading genes on plasmid NAH7 are on a defective
RT transposon.";
RL Mol. Gen. Genet. 223:33-39(1990).
RN [2] {ECO:0000313|EMBL:BAE92162.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G7 {ECO:0000313|EMBL:BAE92162.1};
RC PLASMID=NAH7 {ECO:0000313|EMBL:BAE92162.1};
RX PubMed=16707697; DOI=10.1128/JB.00185-06;
RA Sota M., Yano H., Ono A., Miyazaki R., Ishii H., Genka H., Top E.M.,
RA Tsuda M.;
RT "Genomic and functional analysis of the IncP-9 naphthalene-catabolic
RT plasmid NAH7 and its transposon Tn4655 suggests catabolic gene spread by a
RT tyrosine recombinase.";
RL J. Bacteriol. 188:4057-4067(2006).
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}.
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DR EMBL; AB237655; BAE92162.1; -; Genomic_DNA.
DR RefSeq; WP_011475383.1; NC_007926.1.
DR RefSeq; YP_534828.1; NC_007926.1.
DR AlphaFoldDB; Q1XGL4; -.
DR SMR; Q1XGL4; -.
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:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 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:BAE92162.1};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000313|EMBL:BAE92162.1}.
SQ SEQUENCE 331 AA; 36637 MW; E71E285301F56DAD CRC64;
MLNKVIKTTR LTAEDINGAW TIMPTPSTPD ASDWRSTNTV DLDETARIVE ELIAAGVNGI
LSMGTFGECA TLTWEEKRDY VSTVVETIRG RVPYFCGTTA LNTREVIRQT RELIDIGANG
TMLGVPMWVK MDLPTAVQFY RDVAGAVPEA AIAIYANPEA FKFDFPRPFW AEMSKIPQVV
TAKYLGIGML DLDLKLAPNI RFLPHEDDYY AAARINPERI TAFWSSGAMC GPATAIMLRD
EVERAKSTGD WIKAKAISDD MRAADSTLFP RGDFSEFSKY NIGLEKARMD AAGWLKAGPC
RPPYNLVPED YLVGAQKSGK AWAALHAKYS K
//
