ID   TPHB_COMTE              Reviewed;         315 AA.
AC   Q5D0X4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase;
DE            Short=DCD dehydrogenase;
DE            EC=1.3.1.53;
DE   AltName: Full=Terephthalate dihydrodiol dehydrogenase;
GN   Name=tphB;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE TEREPHTHALATE
RP   DEGRADATION.
RC   STRAIN=YZW-D;
RX   PubMed=8565920; DOI=10.2307/3432469;
RA   Wang Y.Z., Zhou Y., Zylstra G.J.;
RT   "Molecular analysis of isophthalate and terephthalate degradation by
RT   Comamonas testosteroni YZW-D.";
RL   Environ. Health Perspect. 103:9-12(1995).
CC   -!- FUNCTION: Involved in the degradation of terephthalate (TPA) via the
CC       protocatechuate (PCA) 4,5-cleavage pathway. Catalyzes the
CC       dehydrogenation of 1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate
CC       (DCD) to yield protocatechuate (PCA) (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:8565920}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate +
CC         NAD(+) = 3,4-dihydroxybenzoate + CO2 + NADH; Xref=Rhea:RHEA:10744,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:36241, ChEBI:CHEBI:57412,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.53;
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR   EMBL; AY923836; AAX18943.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5D0X4; -.
DR   SMR; Q5D0X4; -.
DR   GO; GO:0047120; F:(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0018963; P:phthalate metabolic process; ISS:UniProtKB.
DR   InterPro; IPR005255; PdxA_fam.
DR   PANTHER; PTHR30004; PTHR30004; 1.
DR   Pfam; PF04166; PdxA; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..315
FT                   /note="1,2-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate
FT                   dehydrogenase"
FT                   /id="PRO_0000418982"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  32887 MW;  40FCBAD402DD3C79 CRC64;
     MTIVHRRLAL AIGDPHGIGP EIALKALQQL SATERSLIKV YGPWSALEQA AQICQMESLL
     QDLIHEEAGS LAQPAQWGEI TPQAGLSTVQ SATAAIRACE NGEVDAVIAC PHHETAIHRA
     GIAFSGYPSL LANVLGMNED EVFLMLVGAG LRIVHVTLHE SVRSALERLS PQLVVDAVDA
     AVQTCTLLGV PKPQVAVFGI NPHASEGQLF GLEDSQITAP AVETLRKCGL AVDGPMGADM
     VLAQRKHDLY VAMLHDQGHI PIKLLAPNGA SALSIGGRVV LSSVGHGSAM DIAGRGVADS
     TALLRTIALL GAQPG