BPHA2_RHOJR
ID BPHA2_RHOJR Reviewed; 187 AA.
AC Q53123;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Biphenyl 2,3-dioxygenase subunit beta {ECO:0000305};
DE EC=1.14.12.18 {ECO:0000269|PubMed:17420585};
DE AltName: Full=Biphenyl dioxygenase system, oxygenase component subunit beta {ECO:0000305};
DE Short=BDO, oxygenase component subunit beta {ECO:0000305};
DE AltName: Full=Terminal oxygenase component of biphenyl dioxygenase, small subunit {ECO:0000303|PubMed:15342255};
GN Name=bphA2 {ECO:0000303|PubMed:7793929};
GN Synonyms=bphAb {ECO:0000312|EMBL:ABG99106.1};
GN OrderedLocusNames=RHA1_ro08059 {ECO:0000312|EMBL:ABG99106.1};
OS Rhodococcus jostii (strain RHA1).
OG Plasmid pRHL1 {ECO:0000312|EMBL:ABG99106.1}.
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, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT.
RC STRAIN=RHA1;
RX PubMed=15342255; DOI=10.1016/j.jmb.2004.07.062;
RA Furusawa Y., Nagarajan V., Tanokura M., Masai E., Fukuda M., Senda T.;
RT "Crystal structure of the terminal oxygenase component of biphenyl
RT dioxygenase derived from Rhodococcus sp. strain RHA1.";
RL J. Mol. Biol. 342:1041-1052(2004).
CC -!- FUNCTION: Part of the oxygenase 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. Can
CC also use naphtalene and 4-chlorobiphenyl (4-CB) as substrates, as well
CC as some polychlorinated biphenyls (PCB) such as 2,2'-dichlorobiphenyl,
CC 2,3-dichlorobiphenyl and 2,5,2'-trichlorobiphenyl. Exhibits weak
CC activity toward dibenzofuran and dibenzo-p-dioxin. Electrons are
CC transferred from NADH to the [2Fe-2S] cluster in BphA1 via FAD of BphA4
CC and [2Fe-2S] cluster of BphA3. {ECO:0000269|PubMed:17420585,
CC ECO:0000303|PubMed:7793929}.
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 Evidence={ECO:0000269|PubMed:17420585};
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 1/4.
CC {ECO:0000303|PubMed:7793929}.
CC -!- SUBUNIT: Heterohexamer consisting of three BphA1 subunits and three
CC BphA2 subunits. The multicomponent biphenyl dioxygenase system is
CC composed of a ferredoxin reductase (BphA4), a ferredoxin (BphA3), and a
CC terminal oxygenase (BphA1A2). {ECO:0000269|PubMed:15342255,
CC ECO:0000303|PubMed:17420585}.
CC -!- INTERACTION:
CC Q53123; Q53122: bphA1; NbExp=2; IntAct=EBI-1040088, EBI-1040100;
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 beta subunit family. {ECO:0000305}.
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DR EMBL; D32142; BAA06869.1; -; Genomic_DNA.
DR EMBL; CP000432; ABG99106.1; -; Genomic_DNA.
DR RefSeq; WP_011599001.1; NC_008269.1.
DR PDB; 1ULI; X-ray; 2.20 A; B/D/F=1-187.
DR PDB; 1ULJ; X-ray; 2.60 A; B/D/F=1-187.
DR PDBsum; 1ULI; -.
DR PDBsum; 1ULJ; -.
DR AlphaFoldDB; Q53123; -.
DR SMR; Q53123; -.
DR IntAct; Q53123; 1.
DR EnsemblBacteria; ABG99106; ABG99106; RHA1_ro08059.
DR KEGG; rha:RHA1_ro08059; -.
DR PATRIC; fig|101510.16.peg.7406; -.
DR HOGENOM; CLU_102527_1_1_11; -.
DR OMA; DSAWSEN; -.
DR UniPathway; UPA00155; UER00250.
DR EvolutionaryTrace; Q53123; -.
DR Proteomes; UP000008710; Plasmid pRHL1.
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; Plasmid; Reference proteome.
FT CHAIN 1..187
FT /note="Biphenyl 2,3-dioxygenase subunit beta"
FT /id="PRO_0000430660"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:1ULI"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1ULI"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1ULI"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:1ULI"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 108..120
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 126..139
FT /evidence="ECO:0007829|PDB:1ULI"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 143..157
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1ULJ"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:1ULI"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:1ULI"
SQ SEQUENCE 187 AA; 22020 MW; 896AE86BC80F215C CRC64;
MIDAESPTTA FRTKPAPVDP SLQHEIEQFY YWEAKLLNDR RFQEWFDLLA EDIHYFMPIR
TTRIMRETAQ EYSGAREYAH FDDNAQMMRG RLRKITSDVS WSENPASRTR HVISNVMIVD
GEKPGEYHVS SVFIVYRNRL ERQLDIFAGE RKDILRRTGS EAGFELAKRT ILIDQSTILS
NNLSFFF
