ID   BPHB_COMTE              Reviewed;         281 AA.
AC   Q46381; Q46376;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase;
DE            EC=1.3.1.56;
DE   AltName: Full=Biphenyl-2,3-dihydro-2,3-diol dehydrogenase;
DE   AltName: Full=Biphenyl-cis-diol dehydrogenase;
DE   AltName: Full=2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase;
DE   AltName: Full=2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase;
DE   AltName: Full=B2,3D;
GN   Name=bphB;
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 CHARACTERIZATION.
RC   STRAIN=B-356;
RX   MEDLINE=96316386; PubMed=8702262;
RA   Sylvestre M., Hurtubise Y., Barriault D., Bergeron J., Ahmad D.;
RT   "Characterization of active recombinant 2,3-dihydro-2,3-
RT   dihydroxybiphenyl dehydrogenase from Comamonas testosteroni B-356 and
RT   sequence of the encoding gene (bphB).";
RL   Appl. Environ. Microbiol. 62:2710-2715(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC   STRAIN=B-356;
RX   MEDLINE=97045812; PubMed=8890734; DOI=10.1016/0378-1119(96)00039-X;
RA   Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D.,
RA   Shareck F., Barriault D., Guillemette I., Juteau J.-M.;
RT   "Sequencing of Comamonas testosteroni strain B-356-
RT   biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships
RT   among Gram-negative bacterial biphenyl dioxygenases.";
RL   Gene 174:195-202(1996).
CC   -!- CATALYTIC ACTIVITY: Cis-3-phenylcyclohexa-3,5-diene-1,2-diol +
CC       NAD(+) = biphenyl-2,3-diol + NADH.
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-
CC       2,4-pentadienoic acid and benzoic acid from biphenyl: step 2/4.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; U57451; AAB18304.1; -; mRNA.
DR   EMBL; U47637; AAC44530.1; -; Genomic_DNA.
DR   PIR; PC4213; PC4213.
DR   HSSP; P47227; 1BDB.
DR   SMR; Q46381; 1-276.
DR   BRENDA; 1.3.1.56; 4566.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0018509; F:cis-2,3-dihydrobiphenyl-2,3-diol dehydrogen...; IEA:EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017711; BphB_TodD.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR19410; ADH_short_C2; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   TIGRFAMs; TIGR03325; BphB_TodD; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   CHAIN         1    281       Cis-2,3-dihydrobiphenyl-2,3-diol
FT                                dehydrogenase.
FT                                /FTId=PRO_0000054532.
FT   NP_BIND      10     34       NAD (By similarity).
FT   ACT_SITE    155    155       Proton acceptor (By similarity).
FT   BINDING     142    142       Substrate (By similarity).
SQ   SEQUENCE   281 AA;  29350 MW;  D50A4CC9167A113E CRC64;
     MKLTGEVALI TGGASGLGRA LVDRFVAEGA RVAVLDKSAE RLRELEVAHG GNAVGVVGDV
     RSLQDQKRAA ERCLAAFGKI DTLIPNAGIW DYSTALADLP EDKIDAAFDD IFHVNVKGYI
     HAVKACLPAL VSSRGSVVFT ISNAGFYPNG GGPLYTATKH AVVGLVRQMA FELAPHVRVN
     GVAPGGMNTD LRGPSSLGLS EQSISSVPLA DMLKSVLPIG RMPALEEYTG AYVFFATRGD
     SLPATGALLN YDGGMGVRGF LTAAGGADLP EKLNINREGQ E
//