BPHE_PARXL
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 03-AUG-2022, entry version 131.
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; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC 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 + H(+) + NADH + O2 = (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};
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DR EMBL; M86348; AAB63426.1; -; Genomic_DNA.
DR EMBL; CP000272; ABE37058.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_040123616.1; NZ_CP008761.1.
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 PDBsum; 2XR8; -.
DR PDBsum; 2XRX; -.
DR PDBsum; 2XSH; -.
DR PDBsum; 2XSO; -.
DR PDBsum; 2YFI; -.
DR PDBsum; 2YFJ; -.
DR PDBsum; 2YFL; -.
DR PDBsum; 5AEU; -.
DR PDBsum; 5AEW; -.
DR AlphaFoldDB; P37334; -.
DR SMR; P37334; -.
DR STRING; 266265.Bxe_C1196; -.
DR EnsemblBacteria; ABE37058; ABE37058; Bxe_C1196.
DR KEGG; bxb:DR64_8609; -.
DR KEGG; bxe:Bxe_C1196; -.
DR PATRIC; fig|266265.5.peg.8946; -.
DR eggNOG; COG5517; Bacteria.
DR OMA; LQAHQFL; -.
DR OrthoDB; 1736098at2; -.
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:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534; PTHR41534; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 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 9..12
FT /evidence="ECO:0007829|PDB:5AEU"
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
