ID   DPDD_ALCFA              Reviewed;         277 AA.
AC   Q9WXG7;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase;
DE            EC=1.3.1.49;
DE   AltName: Full=Cis-phenanthrene dihydrodiol dehydrogenase;
DE            Short=PDD dehydrogenase;
GN   Name=phnB;
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AFK2;
RA   Kiyohara H., Tabata Y., Takizawa N.;
RT   "A phenanthrene degradative gene cluster in Alcaligenes faecalis AFK2.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP   REGULATION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC   STRAIN=AFK2;
RX   DOI=10.1271/bbb1961.52.2621;
RA   Nagao K., Takizawa N., Kiyohara H.;
RT   "Purification and properties of cis-phenanthrene dihydrodiol dehydrogenase
RT   in Alcaligenes faecalis AFK2.";
RL   Agric. Biol. Chem. 52:2621-2623(1988).
CC   -!- FUNCTION: Involved in the degradation of phenanthrene. Catalyzes the
CC       oxidation of cis-phenanthrene dihydrodiol (PDD) to yield
CC       phenanthrenediol. It can use either NAD or NADP as electron acceptor,
CC       however NAD is preferred to NADP. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S,4R)-3,4-dihydrophenanthrene-3,4-diol + NAD(+) = H(+) +
CC         NADH + phenanthrene-3,4-diol; Xref=Rhea:RHEA:16253,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15386, ChEBI:CHEBI:16760,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.49;
CC         Evidence={ECO:0000269|Ref.2};
CC   -!- ACTIVITY REGULATION: Inhibited by heavy metal such as Hg(2+) and by p-
CC       chloromercuribenzoate. {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=210 uM for PDD (at pH 9 and 30 degrees Celsius)
CC         {ECO:0000269|Ref.2};
CC         KM=580 uM for NAD (at pH 9 and 30 degrees Celsius)
CC         {ECO:0000269|Ref.2};
CC         KM=6.3 mM for NADP (at pH 9 and 30 degrees Celsius)
CC         {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 9. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB024945; BAA76322.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WXG7; -.
DR   SMR; Q9WXG7; -.
DR   GO; GO:0018507; F:cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042216; P:phenanthrene catabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..277
FT                   /note="Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase"
FT                   /id="PRO_0000424348"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         10..37
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  28827 MW;  DE3701AB9B96D7DC CRC64;
     MAWLEGQSVF LTGGVAGLGR ALVKRLVEEG ANVTVLDRNA RGLDELVESF KGRVAGSPGD
     VRNLADNRKA VELAVERFGK LDTFNRQRRH LGLLCPPCRP AGRCHQRSFD EVIGINLMGY
     VMGIKAAAPA LVRSRGSVIL TLSSSAFYAG GGGVLYTVAK HAAVGLIKQA AHELAPYVRV
     NGVAPGGIAS DLRGPKSLGM GEQSITSVPL ADLVKDIAPI GRLSDTEEYT GSYVYLASAR
     NSAPATGVII NCDGGMGVRS VLGPASGGKG LLEKFGG