ID   TPHB_COMSP              Reviewed;         315 AA.
AC   Q3C1E1;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 39.
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=tphBI;
OS   Comamonas sp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas; unclassified Comamonas.
OX   NCBI_TaxID=34028;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A DCD DEHYDROGENASE AND IN
RP   THE TEREPHTHALATE DEGRADATION, AND CATALYTIC ACTIVITY.
RC   STRAIN=E6;
RX   PubMed=16517628; DOI=10.1128/aem.72.3.1825-1832.2006;
RA   Sasoh M., Masai E., Ishibashi S., Hara H., Kamimura N., Miyauchi K.,
RA   Fukuda M.;
RT   "Characterization of the terephthalate degradation genes of Comamonas sp.
RT   strain E6.";
RL   Appl. Environ. Microbiol. 72:1825-1832(2006).
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). {ECO:0000269|PubMed:16517628}.
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         Evidence={ECO:0000269|PubMed:16517628};
CC   -!- SIMILARITY: Belongs to the PdxA family. {ECO:0000305}.
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DR   EMBL; AB238678; BAE47079.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3C1E1; -.
DR   SMR; Q3C1E1; -.
DR   GO; GO:0047120; F:(3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase activity; IDA: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; IDA: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_0000418983"
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;  32939 MW;  01951ACA51F1BE37 CRC64;
     MTIVHRRLAL AIGDPHGIGP EIALKALRQL SANERSLIKV YGPWSALEQA AQICQMESLL
     QDLIHEEAGS LAQPAQWGEI TPQAGLSTVQ SATAAIRACE NGEVDAVIAC PHHETAIHRA
     GIAFSGYPSL LANVLGMNED QVFLMLVGAG LRIVHVTLHE SVRSALERLS PQLVVNAVQA
     AVQTCTLLGV PKPQVAVFGI NPHASEGQLF GLEDSQITAP AVETLRKCGL AVDGPMGADM
     VLAQRKHDLY VAMLHDQGHI PIKLLAPNGA SALSIGGRVV LSSVGHGSAM DIAGRGVADS
     TALLRTIALL GAQPG