BPHA_PARXL
ID BPHA_PARXL Reviewed; 459 AA.
AC P37333; Q13FT0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Biphenyl dioxygenase subunit alpha;
DE EC=1.14.12.18;
DE AltName: Full=Biphenyl 2,3-dioxygenase;
GN Name=bphA; OrderedLocusNames=Bxeno_C1131; ORFNames=Bxe_C1197;
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 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).
RN [3]
RP PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION.
RX PubMed=7592331; DOI=10.1128/jb.177.20.5834-5839.1995;
RA Haddock J.D., Gibson D.T.;
RT "Purification and characterization of the oxygenase component of biphenyl
RT 2,3-dioxygenase from Pseudomonas sp. strain LB400.";
RL J. Bacteriol. 177:5834-5839(1995).
RN [4]
RP ERRATUM OF PUBMED:7592331.
RA Haddock J.D., Gibson D.T.;
RL J. Bacteriol. 178:2158-2158(1996).
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 -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Note=Binds 1 [2Fe-2S] cluster per subunit.;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Note=Binds 1 Fe cation per subunit.;
CC -!- PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-
CC pentadienoate and benzoate from biphenyl: step 1/4.
CC -!- SUBUNIT: Heterohexamer consisting of three BphA subunits and three 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 alpha subunit family. {ECO:0000305}.
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DR EMBL; M86348; AAB63425.1; -; Genomic_DNA.
DR EMBL; CP000272; ABE37059.1; -; Genomic_DNA.
DR RefSeq; WP_011494299.1; NZ_CP008761.1.
DR PDB; 2XR8; X-ray; 2.49 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-459.
DR PDB; 2XRX; X-ray; 2.42 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-459.
DR PDB; 2XSH; X-ray; 2.29 A; A/C/E/G/I/K=1-459.
DR PDB; 2XSO; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-459.
DR PDB; 2YFI; X-ray; 2.15 A; A/C/E/G/I/K=1-459.
DR PDB; 2YFJ; X-ray; 2.15 A; A/C/E/G/I/K=1-459.
DR PDB; 2YFL; X-ray; 2.60 A; A/C/E/G/I/K=1-459.
DR PDB; 5AEU; X-ray; 2.49 A; A/C/E/G=1-459.
DR PDB; 5AEW; X-ray; 1.88 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-459.
DR PDBsum; 2XR8; -.
DR PDBsum; 2XRX; -.
DR PDBsum; 2XSH; -.
DR PDBsum; 2XSO; -.
DR PDBsum; 2YFI; -.
DR PDBsum; 2YFJ; -.
DR PDBsum; 2YFL; -.
DR PDBsum; 5AEU; -.
DR PDBsum; 5AEW; -.
DR AlphaFoldDB; P37333; -.
DR SMR; P37333; -.
DR STRING; 266265.Bxe_C1197; -.
DR EnsemblBacteria; ABE37059; ABE37059; Bxe_C1197.
DR KEGG; bxb:DR64_8608; -.
DR KEGG; bxe:Bxe_C1197; -.
DR PATRIC; fig|266265.5.peg.8947; -.
DR eggNOG; COG4638; Bacteria.
DR OMA; AQVGYNE; -.
DR OrthoDB; 275867at2; -.
DR BRENDA; 1.14.12.18; 7691.
DR UniPathway; UPA00155; UER00250.
DR EvolutionaryTrace; P37333; -.
DR Proteomes; UP000001817; Chromosome 3.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018687; F:biphenyl 2,3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7592331"
FT CHAIN 2..459
FT /note="Biphenyl dioxygenase subunit alpha"
FT /id="PRO_0000085046"
FT DOMAIN 58..156
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 100
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 102
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 120
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 123
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT HELIX 21..25
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:2XR8"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:2YFI"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 232..239
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 281..297
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 319..326
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 350..359
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 364..377
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 385..398
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:5AEW"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:2YFL"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:5AEW"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 436..450
FT /evidence="ECO:0007829|PDB:5AEW"
FT HELIX 454..457
FT /evidence="ECO:0007829|PDB:5AEW"
SQ SEQUENCE 459 AA; 51513 MW; 54794B7146730A8F CRC64;
MSSAIKEVQG APVKWVTNWT PEAIRGLVDQ EKGLLDPRIY ADQSLYELEL ERVFGRSWLL
LGHESHVPET GDFLATYMGE DPVVMVRQKD KSIKVFLNQC RHRGMRICRS DAGNAKAFTC
SYHGWAYDIA GKLVNVPFEK EAFCDKKEGD CGFDKAEWGP LQARVATYKG LVFANWDVQA
PDLETYLGDA RPYMDVMLDR TPAGTVAIGG MQKWVIPCNW KFAAEQFCSD MYHAGTTTHL
SGILAGIPPE MDLSQAQIPT KGNQFRAAWG GHGSGWYVDE PGSLLAVMGP KVTQYWTEGP
AAELAEQRLG HTGMPVRRMV GQHMTIFPTC SFLPTFNNIR IWHPRGPNEI EVWAFTLVDA
DAPAEIKEEY RRHNIRNFSA GGVFEQDDGE NWVEIQKGLR GYKAKSQPLN AQMGLGRSQT
GHPDFPGNVG YVYAEEAARG MYHHWMRMMS EPSWATLKP
