BPHE_COMTE
ID BPHE_COMTE Reviewed; 186 AA.
AC Q46373;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Biphenyl dioxygenase subunit beta;
DE EC=1.14.12.18;
DE AltName: Full=Biphenyl 2,3-dioxygenase;
GN Name=bphE;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 -!- 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 3 BphA subunits and 3 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 ---------------------------------------------------------------------------
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; U47637; AAC44527.1; -; Genomic_DNA.
DR PIR; JC4994; JC4994.
DR PDB; 3GZX; X-ray; 1.58 A; B=1-186.
DR PDB; 3GZY; X-ray; 1.62 A; B=1-186.
DR PDBsum; 3GZX; -.
DR PDBsum; 3GZY; -.
DR AlphaFoldDB; Q46373; -.
DR SMR; Q46373; -.
DR UniPathway; UPA00155; UER00250.
DR EvolutionaryTrace; Q46373; -.
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; NAD;
KW Oxidoreductase.
FT CHAIN 1..186
FT /note="Biphenyl dioxygenase subunit beta"
FT /id="PRO_0000085069"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 84..94
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 107..119
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 125..138
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 142..156
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 162..173
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3GZX"
SQ SEQUENCE 186 AA; 21556 MW; 7A307552B4127A00 CRC64;
MISTPLSKEF EWPAKPVSLE LQHQVEQFYY REAQLLDHHA FQAWFALLAE DIHYWMPIRT
VRTAREQGLE YVPAGANAHF DDTHATMYGR IRQKTSDLNW AEDPPSRTRH LVSNVIVREM
DTPGTLEVAS AFLLYRSRLE RQVDVFAGER RDVLRIADNP LGFQIAKRTI ILDQSTVLAN
NLSVFF
