ID   NAHD_PSEU8              Reviewed;         212 AA.
AC   Q52462;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=2-hydroxychromene-2-carboxylate isomerase;
DE            Short=HCCA isomerase;
DE            EC=5.99.1.4;
GN   Name=doxJ;
OS   Pseudomonas sp. (strain C18).
OG   Plasmid unnamed.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=69011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=C18; PLASMID=unnamed;
RX   PubMed=8226631; DOI=10.1128/jb.175.21.6890-6901.1993;
RA   Denome S.A., Stanley D.C., Olson E.S., Young K.D.;
RT   "Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains:
RT   complete DNA sequence of an upper naphthalene catabolic pathway.";
RL   J. Bacteriol. 175:6890-6901(1993).
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       (Probable). {ECO:0000305|PubMed:8226631}.
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   -!- COFACTOR:
CC       Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000250};
CC   -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC   -!- MISCELLANEOUS: DoxH and doxJ encode different enzymes that may have
CC       interchangeable functions. {ECO:0000305|PubMed:8226631}.
CC   -!- MISCELLANEOUS: Encoded on an unnamed 75 kb plasmid.
CC       {ECO:0000305|PubMed:8226631}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. NadH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA16133.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; M60405; AAA16133.2; ALT_INIT; Genomic_DNA.
DR   PIR; I49343; I49343.
DR   AlphaFoldDB; Q52462; -.
DR   SMR; Q52462; -.
DR   UniPathway; UPA00082; -.
DR   GO; GO:0018845; F:2-hydroxychromene-2-carboxylate isomerase activity; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:1901170; P:naphthalene catabolic process; IMP: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   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; Isomerase; Plasmid.
FT   CHAIN           1..212
FT                   /note="2-hydroxychromene-2-carboxylate isomerase"
FT                   /id="PRO_0000096701"
FT   ACT_SITE        24
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         192..195
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  24039 MW;  5EF96A619913DB4F CRC64;
     MLLCRLLFLE CLIVIVDFYF DFLSPFSYLA NHRLSKLAQD YGFSIRYYAI DLARVKIAIG
     NVGPSNRDLI VKLDYLKVDL QRWAELYEIP LVFPANYNSR RMNTGLYYSG AMAQTGAYVN
     VVFNAVWGDG IAPDLESLPA LVSEKLGWDR SAFEDFISSD AATERYDEQT HAAIERKVFG
     VPTMFLGDEM WWGNDRLFML ENAVGGAPVN GE