NAHE1_PSEPU
ID NAHE1_PSEPU Reviewed; 331 AA.
AC Q51947;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase;
DE Short=THBPA hydratase-aldolase;
DE EC=4.1.2.45;
DE AltName: Full=2'-hydroxybenzalpyruvate aldolase;
GN Name=nahE;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid NAH7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND NOMENCLATURE.
RC STRAIN=ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 /
RC Biotype A;
RX PubMed=8002605; DOI=10.1128/jb.176.24.7757-7762.1994;
RA Eaton R.W.;
RT "Organization and evolution of naphthalene catabolic pathways: sequence of
RT the DNA encoding 2-hydroxychromene-2-carboxylate isomerase and trans-o-
RT hydroxybenzylidenepyruvate hydratase-aldolase from the NAH7 plasmid.";
RL J. Bacteriol. 176:7757-7762(1994).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 /
RC Biotype A;
RX PubMed=1447127; DOI=10.1128/jb.174.23.7542-7554.1992;
RA Eaton R.W., Chapman P.J.;
RT "Bacterial metabolism of naphthalene: construction and use of recombinant
RT bacteria to study ring cleavage of 1,2-dihydroxynaphthalene and subsequent
RT reactions.";
RL J. Bacteriol. 174:7542-7554(1992).
CC -!- FUNCTION: Involved in the naphthalene upper catabolic pathway.
CC Catalyzes the transformation of trans-O-hydroxybenzylidenepyruvate
CC (THBPA) to salicylaldehyde and pyruvate. The reaction is reversible.
CC Can also use substrate which carry trans-alpha,beta-unsaturated keto
CC acid side chain and adjacent hydroxyl group such as trans-4-(3-hydroxy-
CC 2-thianaphthenyl)-2-oxo-but-3-enoate, trans-4-(3-hydroxy-2-
CC benzofuranyl)-2-oxobut-3-enoate, and trans-4-(3-hydroxy-2-thienyl)-2-
CC oxobut-3-enoate. {ECO:0000269|PubMed:1447127,
CC ECO:0000269|PubMed:8002605}.
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:0000269|PubMed:1447127};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000305}.
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DR EMBL; U09057; AAA66357.1; -; Genomic_DNA.
DR PIR; B55552; B55552.
DR RefSeq; WP_011475383.1; NC_007926.1.
DR RefSeq; YP_534828.1; NC_007926.1.
DR PDB; 6DAO; X-ray; 1.94 A; A/B=1-331.
DR PDBsum; 6DAO; -.
DR AlphaFoldDB; Q51947; -.
DR SMR; Q51947; -.
DR KEGG; ag:AAA66357; -.
DR BRENDA; 4.1.2.45; 5092.
DR UniPathway; UPA00082; -.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:UniProtKB.
DR GO; GO:0018813; F:trans-o-hydroxybenzylidenepyruvate hydratase-aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:1901170; P:naphthalene catabolic process; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR PANTHER; PTHR12128; PTHR12128; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Lyase; Plasmid; Pyruvate.
FT CHAIN 1..331
FT /note="Trans-O-hydroxybenzylidenepyruvate hydratase-
FT aldolase"
FT /id="PRO_0000096702"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:6DAO"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:6DAO"
FT TURN 65..71
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:6DAO"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:6DAO"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 233..248
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:6DAO"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 281..292
FT /evidence="ECO:0007829|PDB:6DAO"
FT HELIX 309..328
FT /evidence="ECO:0007829|PDB:6DAO"
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
