BPHB_PARXL
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 03-AUG-2022, entry version 152.
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; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC 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 (2.0 ANGSTROMS) 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 + 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 -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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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; NZ_CP008761.1.
DR PDB; 1BDB; X-ray; 2.00 A; A=1-277.
DR PDBsum; 1BDB; -.
DR AlphaFoldDB; P47227; -.
DR SMR; P47227; -.
DR STRING; 266265.Bxe_C1192; -.
DR EnsemblBacteria; ABE37054; ABE37054; Bxe_C1192.
DR KEGG; bxb:DR64_8613; -.
DR KEGG; bxe:Bxe_C1192; -.
DR eggNOG; COG1028; Bacteria.
DR OMA; VFHINVK; -.
DR OrthoDB; 1356861at2; -.
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: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;
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..115
FT /evidence="ECO:0007829|PDB:1BDB"
FT HELIX 117..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
