BPHB_COMTE
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 03-AUG-2022, entry version 105.
DE RecName: Full=Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase;
DE EC=1.3.1.56;
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;
DE AltName: Full=Biphenyl-2,3-dihydro-2,3-diol dehydrogenase;
DE AltName: Full=Biphenyl-cis-diol dehydrogenase;
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 PubMed=8702262; DOI=10.1128/aem.62.8.2710-2715.1996;
RA Sylvestre M., Hurtubise Y., Barriault D., Bergeron J., Ahmad D.;
RT "Characterization of active recombinant 2,3-dihydro-2,3-dihydroxybiphenyl
RT dehydrogenase from Comamonas testosteroni B-356 and sequence of the
RT 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 PubMed=8890734; DOI=10.1016/0378-1119(96)00039-x;
RA Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D., Shareck F.,
RA Barriault D., Guillemette I., Juteau J.-M.;
RT "Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl
RT dioxygenase genes: evolutionary relationships among Gram-negative bacterial
RT biphenyl dioxygenases.";
RL Gene 174:195-202(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) =
CC biphenyl-2,3-diol + H(+) + NADH; Xref=Rhea:RHEA:17033,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16205, ChEBI:CHEBI:32922,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.56;
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 2/4.
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; U57451; AAB18304.1; -; mRNA.
DR EMBL; U47637; AAC44530.1; -; Genomic_DNA.
DR PIR; PC4213; PC4213.
DR PDB; 2Y93; X-ray; 2.22 A; A/B=1-281.
DR PDB; 2Y99; X-ray; 2.50 A; A/B=1-281.
DR PDB; 3ZV3; X-ray; 2.90 A; A/B=1-281.
DR PDB; 3ZV4; X-ray; 1.80 A; A/B=1-281.
DR PDB; 3ZV5; X-ray; 2.40 A; A/B=1-281.
DR PDB; 3ZV6; X-ray; 2.14 A; A/B=1-281.
DR PDBsum; 2Y93; -.
DR PDBsum; 2Y99; -.
DR PDBsum; 3ZV3; -.
DR PDBsum; 3ZV4; -.
DR PDBsum; 3ZV5; -.
DR PDBsum; 3ZV6; -.
DR AlphaFoldDB; Q46381; -.
DR SMR; Q46381; -.
DR KEGG; ag:AAB18304; -.
DR BRENDA; 1.3.1.56; 1590.
DR UniPathway; UPA00155; UER00251.
DR EvolutionaryTrace; Q46381; -.
DR GO; GO:0018509; F:cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR017711; BphB_TodD.
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 PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03325; BphB_TodD; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT CHAIN 1..281
FT /note="Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase"
FT /id="PRO_0000054532"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3ZV4"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3ZV6"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:3ZV4"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2Y93"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3ZV4"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 117..133
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 153..173
FT /evidence="ECO:0007829|PDB:3ZV4"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3ZV6"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3ZV6"
FT HELIX 209..215
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:3ZV4"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3ZV4"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:3ZV4"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:3ZV4"
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
