ID BPHB_PARXL Reviewed; 277 AA. AC P47227; Q13FT5; Q52435; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 04-NOV-2026, entry version 168. 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=Biphenyl-2,3-dihydro-2,3-diol dehydrogenase; DE AltName: Full=Biphenyl-cis-diol dehydrogenase; GN Name=bphB; OrderedLocusNames=Bxeno_C1126; ORFNames=Bxe_C1192; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8344527; DOI=10.1016/0378-1119(93)90345-4; RA Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.; RT "Genetic analysis of a Pseudomonas locus encoding a pathway for RT biphenyl/polychlorinated biphenyl degradation."; RL Gene 130:47-55(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome RT shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. RX PubMed=1569021; DOI=10.1128/jb.174.9.2903-2912.1992; RA Erickson B.D., Mondello F.J.; RT "Nucleotide sequencing and transcriptional mapping of the genes encoding RT biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading RT enzyme in Pseudomonas strain LB400."; RL J. Bacteriol. 174:2903-2912(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH NAD. RX PubMed=9655331; DOI=10.1002/pro.5560070603; RA Huelsmeyer M., Hecht H.-J., Niefind K., Hofer B., Eltis L.D., Timmis K.N., RA Schomburg D.; RT "Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a RT PCB degrader at 2.0-A resolution."; RL Protein Sci. 7:1286-1293(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) = CC biphenyl-2,3-diol + NADH + H(+); 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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66122; CAA46909.1; -; Genomic_DNA. DR EMBL; CP000272; ABE37054.1; -; Genomic_DNA. DR EMBL; M86348; AAB63430.2; -; Genomic_DNA. DR PIR; JN0814; JN0814. DR RefSeq; WP_011494296.1; NC_007953.1. DR PDB; 1BDB; X-ray; 2.00 A; A=1-277. DR AlphaFoldDB; P47227; -. DR SMR; P47227; -. DR STRING; 266265.Bxe_C1192; -. DR KEGG; bxb:DR64_8613; -. DR KEGG; bxe:Bxe_C1192; -. DR eggNOG; COG1028; Bacteria. DR OMA; ACGGMNT; -. DR OrthoDB; 9809287at2; -. DR BRENDA; 1.3.1.56; 5085. DR UniPathway; UPA00155; UER00251. DR EvolutionaryTrace; P47227; -. DR Proteomes; UP000001817; Chromosome 3. DR GO; GO:0018509; F:cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:TreeGrafter. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProtKB-ARBA. DR CDD; cd05348; BphB-like_SDR_c; 1. DR FunFam; 3.40.50.720:FF:000084; Short-chain dehydrogenase reductase; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR047950; BphB-like_SDR. 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 NCBIfam; TIGR03325; BphB_TodD; 1. DR NCBIfam; NF004849; hcaB; 1. DR PANTHER; PTHR43008; BENZIL REDUCTASE; 1. DR PANTHER; PTHR43008:SF4; CHAIN DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G08710)-RELATED; 1. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00081; GDHRDH. DR PRINTS; PR00080; SDRFAMILY. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00061; ADH_SHORT; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..277 FT /note="Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase" FT /id="PRO_0000054531" FT ACT_SITE 155 FT /note="Proton acceptor" FT BINDING 9..36 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:9655331" FT BINDING 59 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:9655331" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 159 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:9655331" FT TURN 2..5 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 7..11 FT /evidence="ECO:0007829|PDB:1BDB" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 16..27 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 63..77 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 96..98 FT /evidence="ECO:0007829|PDB:1BDB" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 104..112 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 113..117 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 118..133 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 136..140 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 143..145 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 153..173 FT /evidence="ECO:0007829|PDB:1BDB" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 178..184 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 209..213 FT /evidence="ECO:0007829|PDB:1BDB" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 230..236 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 238..241 FT /evidence="ECO:0007829|PDB:1BDB" FT STRAND 248..254 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 255..257 FT /evidence="ECO:0007829|PDB:1BDB" FT HELIX 269..273 FT /evidence="ECO:0007829|PDB:1BDB" SQ SEQUENCE 277 AA; 28901 MW; 00194120BD4E12D1 CRC64; MKLKGEAVLI TGGASGLGRA LVDRFVAEGA KVAVLDKSAE RLAELETDHG DNVLGIVGDV RSLEDQKQAA SRCVARFGKI DTLIPNAGIW DYSTALVDLP EESLDAAFDE VFHINVKGYI HAVKACLPAL VASRGNVIFT ISNAGFYPNG GGPLYTAAKH AIVGLVRELA FELAPYVRVN GVGSGGINSD LRGPSSLGMG SKAISTVPLA DMLKSVLPIG RMPEVEEYTG AYVFFATRGD AAPATGALLN YDGGLGVRGF FSGAGGNDLL EQLNIHP //