ID   BPHG_PARXL              Reviewed;         408 AA.
AC   P37337; Q13FT4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Biphenyl dioxygenase system ferredoxin--NAD(+) reductase component;
DE            EC=1.18.1.3;
GN   Name=bphG; OrderedLocusNames=Bxeno_C1127; ORFNames=Bxe_C1193;
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   SEQUENCE REVISION.
RA   Erickson B.D., Mondello F.J.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
CC   -!- FUNCTION: Part of the electron transfer component of biphenyl
CC       dioxygenase, transfers electrons from ferredoxin (BphF) to NADH.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.18.1.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Xenobiotic degradation; biphenyl degradation.
CC   -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC       subunits of the hydroxylase component (BphA and BphE), a ferredoxin
CC       (BphF) and a ferredoxin reductase (BphG).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin reductase family. {ECO:0000305}.
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DR   EMBL; M86348; AAB63429.1; -; Genomic_DNA.
DR   EMBL; CP000272; ABE37055.1; -; Genomic_DNA.
DR   PIR; F41858; F41858.
DR   RefSeq; WP_003450997.1; NZ_CP008761.1.
DR   AlphaFoldDB; P37337; -.
DR   SMR; P37337; -.
DR   STRING; 266265.Bxe_C1193; -.
DR   EnsemblBacteria; ABE37055; ABE37055; Bxe_C1193.
DR   KEGG; bxb:DR64_8612; -.
DR   KEGG; bxe:Bxe_C1193; -.
DR   eggNOG; COG1251; Bacteria.
DR   OrthoDB; 1149616at2; -.
DR   UniPathway; UPA00155; -.
DR   Proteomes; UP000001817; Chromosome 3.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..408
FT                   /note="Biphenyl dioxygenase system ferredoxin--NAD(+)
FT                   reductase component"
FT                   /id="PRO_0000167653"
FT   BINDING         4..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         145..173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  42954 MW;  8A52BB01688667A9 CRC64;
     MIDTIAIIGA GLAGSTAARA LRAQGYEGRI HLLGDESHQA YDRTTLSKTV LAGEQPEPPA
     ILDSAWYASA HVDVQLGRRV SCLDLANRQI QFESGAPLAY DRLLLATGAR ARRMAIRGGD
     LAGIHTLRDL ADSQALRQAL QPGQSLVIVG GGLIGCEVAT TARKLSVHVT ILEAGDELLV
     RVLGHRTGAW CRAELERMGV RVERNAQAAR FEGQGQVRAV ICADGRRVPA DVVLVSIGAE
     PADELARAAG IACARGVLVD ATGATSCPEV FAAGDVAAWP LRQGGQRSLE TYLNSQMEAE
     IAASAMLSQP VPAPQVPTSW TEIAGHRIQM IGDAEGPGEI VVRGDAQSGQ PIVLLRLLDG
     CVEAATAINA TREFSVATRL VGTRVSVSAE QLQDVGSNLR DLLKAKPN