ID BPHE_PARXL Reviewed; 188 AA. AC P37334; Q13FT1; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 146. DE RecName: Full=Biphenyl dioxygenase subunit beta; DE EC=1.14.12.18; DE AltName: Full=Biphenyl 2,3-dioxygenase; GN Name=bphE; OrderedLocusNames=Bxeno_C1130; ORFNames=Bxe_C1196; 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=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 [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 PROTEIN SEQUENCE OF 2-12, AND CHARACTERIZATION. RX PubMed=7592331; DOI=10.1128/jb.177.20.5834-5839.1995; RA Haddock J.D., Gibson D.T.; RT "Purification and characterization of the oxygenase component of biphenyl RT 2,3-dioxygenase from Pseudomonas sp. strain LB400."; RL J. Bacteriol. 177:5834-5839(1995). RN [4] RP ERRATUM OF PUBMED:7592331. RA Haddock J.D., Gibson D.T.; RL J. Bacteriol. 178:258-258(1996). CC -!- FUNCTION: The beta subunit may be responsible for the substrate CC specificity of the enzyme. CC -!- CATALYTIC ACTIVITY: CC Reaction=biphenyl + NADH + O2 + H(+) = (2R,3S)-3-phenylcyclohexa-3,5- CC diene-1,2-diol + NAD(+); Xref=Rhea:RHEA:18165, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17097, ChEBI:CHEBI:32922, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.12.18; CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4- CC pentadienoate and benzoate from biphenyl: step 1/4. CC -!- SUBUNIT: Heterohexamer consisting of three BphA subunits and three BphE CC subunits. A ferredoxin (BphF) and a ferredoxin reductase (BphG) must be CC present to obtain activity. CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase CC beta subunit family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=ABE37058.1; Type=Erroneous initiation; Evidence={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; M86348; AAB63426.1; -; Genomic_DNA. DR EMBL; CP000272; ABE37058.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_040123616.1; NC_007953.1. DR PDB; 2XR8; X-ray; 2.49 A; B/D/F/H/J/L/N/P/R/T/V/X=1-188. DR PDB; 2XRX; X-ray; 2.42 A; B/D/F/H/J/L/N/P/R/T/V/X=1-188. DR PDB; 2XSH; X-ray; 2.29 A; B/D/F/H/J/L=1-188. DR PDB; 2XSO; X-ray; 2.20 A; B/D/F/H/J/L/N/P/R/T/V/X=1-188. DR PDB; 2YFI; X-ray; 2.15 A; B/D/F/H/J/L=1-188. DR PDB; 2YFJ; X-ray; 2.15 A; B/D/F/H/J/L=1-188. DR PDB; 2YFL; X-ray; 2.60 A; B/D/F/H/J/L=1-188. DR PDB; 5AEU; X-ray; 2.49 A; B/D/F/H=1-188. DR PDB; 5AEW; X-ray; 1.88 A; B/D/F/H/J/L/N/P/R/T/V/X=1-188. DR AlphaFoldDB; P37334; -. DR SMR; P37334; -. DR STRING; 266265.Bxe_C1196; -. DR KEGG; bxb:DR64_8609; -. DR KEGG; bxe:Bxe_C1196; -. DR PATRIC; fig|266265.5.peg.8946; -. DR eggNOG; COG5517; Bacteria. DR OrthoDB; 7062869at2; -. DR BRENDA; 1.14.12.18; 7691. DR UniPathway; UPA00155; UER00250. DR EvolutionaryTrace; P37334; -. DR Proteomes; UP000001817; Chromosome 3. DR GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0019380; P:3-phenylpropionate catabolic process; IEA:TreeGrafter. DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1. DR Gene3D; 3.10.450.50; -; 1. DR InterPro; IPR032710; NTF2-like_dom_sf. DR InterPro; IPR000391; Rng_hydr_dOase-bsu. DR NCBIfam; NF007479; PRK10069.1; 1. DR PANTHER; PTHR41534:SF2; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE SUBUNIT BETA; 1. DR PANTHER; PTHR41534; BLR3401 PROTEIN; 1. DR Pfam; PF00866; Ring_hydroxyl_B; 1. DR SUPFAM; SSF54427; NTF2-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:7592331" FT CHAIN 2..188 FT /note="Biphenyl dioxygenase subunit beta" FT /id="PRO_0000085068" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 21..39 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 43..47 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 50..59 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 66..71 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 80..84 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 86..97 FT /evidence="ECO:0007829|PDB:5AEW" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 109..121 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 127..140 FT /evidence="ECO:0007829|PDB:5AEW" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 144..158 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 160..175 FT /evidence="ECO:0007829|PDB:5AEW" FT STRAND 177..182 FT /evidence="ECO:0007829|PDB:5AEW" SQ SEQUENCE 188 AA; 22085 MW; 36DBE14E22FEA67B CRC64; MTNPSPHFFK TFEWPSKAAG LELQNEIEQF YYREAQLLDH RAYEAWFALL DKDIHYFMPL RTNRMIREGE LEYSGDQDLA HFDETHETMY GRIRKVTSDV GWAENPPSRT RHLVSNVIVK ETATPDTFEV NSAFILYRNR LERQVDIFAG ERRDVLRRAD NNLGFSIAKR TILLDASTLL SNNLSMFF //