BPHA3_RHOJR
ID BPHA3_RHOJR Reviewed; 107 AA.
AC Q53124; Q0S031;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Biphenyl 2,3-dioxygenase, ferredoxin component {ECO:0000303|PubMed:17420585};
DE AltName: Full=Biphenyl 2,3-dioxygenase, electron transfer component BphA3 {ECO:0000303|PubMed:17420585};
DE AltName: Full=Biphenyl dioxygenase system, ferredoxin component {ECO:0000305};
DE Short=BDO, ferredoxin component {ECO:0000305};
GN Name=bphA3 {ECO:0000303|PubMed:7793929};
GN Synonyms=bphAc {ECO:0000312|EMBL:ABG99105.1};
GN OrderedLocusNames=RHA1_ro08058 {ECO:0000312|EMBL:ABG99105.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000312|EMBL:ABG99105.1}.
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 component of the biphenyl dioxygenase system that
CC catalyzes the stereospecific dihydroxylation of the aromatic ring of
CC biphenyl, yielding a dihydrodiol compound. Is likely involved in
CC biphenyl degradation that allows growth of Rhodococcus sp. strain RHA1
CC on biphenyl as the sole source of carbon and energy. The dioxygenase
CC system can also use naphtalene and 4-chlorobiphenyl (4-CB) as
CC 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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
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 component family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABG99105.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D32142; BAA06870.1; -; Genomic_DNA.
DR EMBL; CP000432; ABG99105.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_050787550.1; NC_008269.1.
DR AlphaFoldDB; Q53124; -.
DR SMR; Q53124; -.
DR EnsemblBacteria; ABG99105; ABG99105; RHA1_ro08058.
DR KEGG; rha:RHA1_ro08058; -.
DR PATRIC; fig|101510.16.peg.7405; -.
DR HOGENOM; CLU_055690_5_2_11; -.
DR UniPathway; UPA00155; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProt.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Plasmid; Reference proteome; Transport.
FT CHAIN 1..107
FT /note="Biphenyl 2,3-dioxygenase, ferredoxin component"
FT /id="PRO_0000430661"
FT DOMAIN 4..99
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 107 AA; 11536 MW; 808A9759954E767F CRC64;
MALTKICSSG DLAPGEMLRF EEGPEPILVC NVGGEFFATQ DTCSHADWAL SEGYLEDDVV
ECTLHWAKFC VRTGKAKALP ACVPLRTFVV KLEGDDVLVD LEGGVTT
