BPHA4_RHOJR
ID BPHA4_RHOJR Reviewed; 413 AA.
AC Q0S032; Q53125;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Biphenyl 2,3-dioxygenase, ferredoxin reductase component {ECO:0000303|PubMed:17420585};
DE EC=1.18.1.3 {ECO:0000303|PubMed:17420585};
DE AltName: Full=Biphenyl 2,3-dioxygenase, electron transfer component BphA4 {ECO:0000303|PubMed:17420585};
DE AltName: Full=Biphenyl dioxygenase system, ferredoxin--NAD(+) reductase component {ECO:0000305};
DE Short=BDO, ferredoxin reductase component {ECO:0000305};
GN Name=bphA4 {ECO:0000303|PubMed:7793929};
GN Synonyms=bphAd {ECO:0000312|EMBL:ABG99104.1};
GN OrderedLocusNames=RHA1_ro08057 {ECO:0000312|EMBL:ABG99104.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000312|EMBL:ABG99104.1}.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC STRAIN=RHA1;
RX PubMed=7793929; DOI=10.1128/aem.61.6.2079-2085.1995;
RA Masai E., Yamada A., Healy J.M., Hatta T., Kimbara K., Fukuda M., Yano K.;
RT "Characterization of biphenyl catabolic genes of gram-positive
RT polychlorinated biphenyl degrader Rhodococcus sp. strain RHA1.";
RL Appl. Environ. Microbiol. 61:2079-2085(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [3]
RP INDUCTION.
RC STRAIN=RHA1;
RX PubMed=15028699; DOI=10.1128/jb.186.7.2134-2146.2004;
RA Takeda H., Yamada A., Miyauchi K., Masai E., Fukuda M.;
RT "Characterization of transcriptional regulatory genes for biphenyl
RT degradation in Rhodococcus sp. strain RHA1.";
RL J. Bacteriol. 186:2134-2146(2004).
RN [4]
RP FUNCTION IN A BDO SYSTEM.
RC STRAIN=RHA1;
RX PubMed=17420585; DOI=10.1271/bbb.60663;
RA Iwasaki T., Takeda H., Miyauchi K., Yamada T., Masai E., Fukuda M.;
RT "Characterization of two biphenyl dioxygenases for biphenyl/PCB degradation
RT in A PCB degrader, Rhodococcus sp. strain RHA1.";
RL Biosci. Biotechnol. Biochem. 71:993-1002(2007).
CC -!- FUNCTION: Ferredoxin reductase component of the biphenyl dioxygenase
CC system that catalyzes the stereospecific dihydroxylation of the
CC aromatic ring of biphenyl, yielding a dihydrodiol compound. Is likely
CC involved in biphenyl degradation that allows growth of Rhodococcus sp.
CC strain RHA1 on biphenyl as the sole source of carbon and energy. The
CC dioxygenase system can also use naphtalene and 4-chlorobiphenyl (4-CB)
CC as substrates, as well as some polychlorinated biphenyls (PCB) such as
CC 2,2'-dichlorobiphenyl, 2,3-dichlorobiphenyl and 2,5,2'-
CC trichlorobiphenyl. It exhibits weak activity toward dibenzofuran and
CC dibenzo-p-dioxin. Electrons are transferred from NADH to the [2Fe-2S]
CC cluster in BphA1 via FAD of BphA4 and [2Fe-2S] cluster of BphA3.
CC {ECO:0000303|PubMed:17420585, ECO:0000303|PubMed:7793929}.
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 Evidence={ECO:0000303|PubMed:17420585};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O85675};
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation.
CC {ECO:0000303|PubMed:7793929}.
CC -!- SUBUNIT: The multicomponent biphenyl dioxygenase system is composed of
CC a ferredoxin reductase (BphA4), a ferredoxin (BphA3), and a terminal
CC oxygenase (BphA1A2). {ECO:0000303|PubMed:17420585}.
CC -!- INDUCTION: Transcription is up-regulated by aromatic compounds
CC including biphenyl, ethylbenzene, benzene, toluene, xylene, cumene,
CC cymene, and chlorinated benzenes. Is under the control of the BphST
CC two-component regulatory system. {ECO:0000269|PubMed:15028699}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000305}.
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DR EMBL; D32142; BAA06871.1; -; Genomic_DNA.
DR EMBL; CP000432; ABG99104.1; -; Genomic_DNA.
DR RefSeq; WP_011598999.1; NC_008269.1.
DR AlphaFoldDB; Q0S032; -.
DR SMR; Q0S032; -.
DR EnsemblBacteria; ABG99104; ABG99104; RHA1_ro08057.
DR KEGG; rha:RHA1_ro08057; -.
DR PATRIC; fig|101510.16.peg.7404; -.
DR HOGENOM; CLU_003291_4_0_11; -.
DR OMA; PADWYDE; -.
DR UniPathway; UPA00155; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
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; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Electron transport; FAD; Flavoprotein;
KW NAD; Oxidoreductase; Plasmid; Reference proteome; Transport.
FT CHAIN 1..413
FT /note="Biphenyl 2,3-dioxygenase, ferredoxin reductase
FT component"
FT /id="PRO_0000430662"
FT BINDING 4..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 145..173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 104
FT /note="L -> H (in Ref. 1; BAA06871)"
SQ SEQUENCE 413 AA; 44024 MW; 26185767DFD490FE CRC64;
MTSDIVVIGG GVAGVTAAQS LRSEGYDGRL VLIGKERELP YDRTALSKAV LAGDLADPPL
LFPADWYDEW QIETVLDRTV LQVDVTRREV LLDGGPWLKV DRVLLATGAS ARVPSFSGSD
LPGVATLRTA DDVHRMRRDW EPGQRLVVVG GGLIGCEVAT TARKLGLEVS ILEASDELLQ
RVLGRRIGGW CRARLMELGI SVVLNTGVAE FKGVDRITTV IGTDGRSFVA DRAIVCVGAE
PETAIAEQSG LACNRGILVN DSGGTAAEGV FAAGDVASWP LLTGGRRSLE TYINSQREAT
AVASAMLGKA VHGPQLPLSW TEMAGHRIQM IGDIEGSGEY VMRGDPDDGP ALLFRLSDGR
VTAAVSVDAP RDFAMATRLV ERGAQVGREV LGDTSMELRE LNRAARERAL IAE
