NAHD_PSEPU
ID NAHD_PSEPU Reviewed; 203 AA.
AC Q51948;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=2-hydroxychromene-2-carboxylate isomerase;
DE Short=HCCA isomerase;
DE EC=5.99.1.4;
GN Name=nahD;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND
RP GLUTATHIONE, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP SUBUNIT.
RX PubMed=17508726; DOI=10.1021/bi700356u;
RA Thompson L.C., Ladner J.E., Codreanu S.G., Harp J., Gilliland G.L.,
RA Armstrong R.N.;
RT "2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione
RT transferase from Pseudomonas putida.";
RL Biochemistry 46:6710-6722(2007).
CC -!- FUNCTION: Involved in the naphthalene catabolic pathway. Catalyzes the
CC reversible glutathione-dependent isomerization of 2-hydroxychromene-2-
CC carboxylate (HCCA) to trans-O-hydroxybenzylidenepyruvate (THBPA).
CC {ECO:0000269|PubMed:1447127, ECO:0000269|PubMed:8002605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxychromene-2-carboxylate = (3E)-4-(2-hydroxyphenyl)-2-
CC oxobut-3-enoate; Xref=Rhea:RHEA:27401, ChEBI:CHEBI:59350,
CC ChEBI:CHEBI:59353; EC=5.99.1.4;
CC Evidence={ECO:0000269|PubMed:1447127};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:1447127, ECO:0000269|PubMed:17508726};
CC Note=Glutathione seems to stabilize the enzyme, which loses activity
CC rapidly in the absence of this compound. {ECO:0000269|PubMed:1447127,
CC ECO:0000269|PubMed:17508726};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for HCCA (at pH 10) {ECO:0000269|PubMed:1447127,
CC ECO:0000269|PubMed:17508726};
CC KM=17 uM for glutathione (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:1447127, ECO:0000269|PubMed:17508726};
CC KM=84 uM for HCCA (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:1447127, ECO:0000269|PubMed:17508726};
CC KM=138 uM for THBPA (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:1447127, ECO:0000269|PubMed:17508726};
CC Note=kcat is 47 sec(-1) for HCCA, 19 sec(-1) for THBPA and 39 sec(-1)
CC for glutathion.;
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:1447127,
CC ECO:0000269|PubMed:17508726};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC -!- SIMILARITY: Belongs to the GST superfamily. NadH family. {ECO:0000305}.
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DR EMBL; U09057; AAA66358.1; -; Genomic_DNA.
DR PIR; C55552; C55552.
DR RefSeq; WP_011475384.1; NC_007926.1.
DR RefSeq; YP_534829.1; NC_007926.1.
DR PDB; 2IMD; X-ray; 1.60 A; A=1-203.
DR PDB; 2IME; X-ray; 1.70 A; A=1-203.
DR PDB; 2IMF; X-ray; 1.30 A; A=1-203.
DR PDBsum; 2IMD; -.
DR PDBsum; 2IME; -.
DR PDBsum; 2IMF; -.
DR AlphaFoldDB; Q51948; -.
DR SMR; Q51948; -.
DR DrugBank; DB06952; (2S)-2-HYDROXY-2H-CHROMENE-2-CARBOXYLIC ACID.
DR DrugBank; DB08636; 2-Hydroxybenzalpyruvate.
DR DrugBank; DB08637; 4-(2-METHOXYPHENYL)-2-OXOBUT-3-ENOIC ACID.
DR KEGG; ag:AAA66358; -.
DR BioCyc; MetaCyc:MON-12808; -.
DR BRENDA; 5.99.1.4; 5092.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; Q51948; -.
DR PRO; PR:Q51948; -.
DR GO; GO:0018845; F:2-hydroxychromene-2-carboxylate isomerase activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR CDD; cd03022; DsbA_HCCA_Iso; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR014440; HCCAis_GSTk.
DR InterPro; IPR044087; NahD-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF006386; HCCAis_GSTk; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Isomerase; Plasmid.
FT CHAIN 1..203
FT /note="2-hydroxychromene-2-carboxylate isomerase"
FT /id="PRO_0000096700"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:17508726"
FT BINDING 11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:17508726"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17508726"
FT BINDING 53..54
FT /ligand="substrate"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17508726"
FT BINDING 168
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:17508726"
FT BINDING 179..182
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 12..28
FT /evidence="ECO:0007829|PDB:2IMF"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 99..115
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:2IMF"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:2IMF"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:2IMF"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:2IMF"
SQ SEQUENCE 203 AA; 23061 MW; E84B56F21C604945 CRC64;
MIVDFYFDFL SPFSYLANQR LSKLAQDYGL TIRYNAIDLA RVKIAIGNVG PSNRDLKVKL
DYLKVDLQRW AQLYGIPLVF PANYNSRRMN IGFYYSGAEA QAAAYVNVVF NAVWGEGIAP
DLESLPALVS EKLGWDRSAF EHFLSSNAAT ERYDEQTHAA IERKVFGVPT MFLGDEMWWG
NDRLFMLESA MGRLCRQNAD LSS
