ID   BPHA_PSEFK              Reviewed;         458 AA.
AC   Q52028;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Biphenyl dioxygenase subunit alpha;
DE            EC=1.14.12.18;
DE   AltName: Full=Biphenyl 2,3-dioxygenase;
GN   Name=bphA; Synonyms=bphA1;
OS   Pseudomonas furukawaii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas;
OC   Pseudomonas oleovorans/pseudoalcaligenes group.
OX   NCBI_TaxID=1149133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 10086 / NBRC 110670 / KF707;
RX   PubMed=1537863; DOI=10.1016/s0021-9258(18)42908-0;
RA   Taira K., Hirose J., Hayashida S., Furukawa K.;
RT   "Analysis of bph operon from the polychlorinated biphenyl-degrading strain
RT   of Pseudomonas pseudoalcaligenes KF707.";
RL   J. Biol. Chem. 267:4844-4853(1992).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250};
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       alpha subunit family. {ECO:0000305}.
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DR   EMBL; M83673; AAA25743.1; -; Genomic_DNA.
DR   PIR; A42409; A42409.
DR   RefSeq; WP_036992472.1; NZ_AP014862.1.
DR   AlphaFoldDB; Q52028; -.
DR   SMR; Q52028; -.
DR   STRING; 1149133.ppKF707_3406; -.
DR   UniPathway; UPA00155; UER00250.
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   3: Inferred from homology;
KW   2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW   Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..458
FT                   /note="Biphenyl dioxygenase subunit alpha"
FT                   /id="PRO_0000085048"
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"
SQ   SEQUENCE   458 AA;  51438 MW;  A6123AD09F97E482 CRC64;
     MSSSIKEVQG APVKWVTNWT PEAIRGLVDQ EKGLLDPRIY ADQSLYELEL ERVFGRSWLL
     LGHESHVPET GDFLATYMGE DPVVMVRQKD KSIKVFLNQC RHRGMRICRS DAGNAKAFTC
     SYHGWAYDIA GKLVNVPFEK EAFCDKKEGD CGFDKAEWGP LQARVATYKG LVFANWDVQA
     PDLETYLGDA RPYMDVMLDR TPAGTVAIGG MQKWVIPCNW KFAAEQFCSD MYHAGTMSHL
     SGILAGMPPE MDLSHAQVPT KGNQFRAGWG GHGSGWFVDE PGMLMAVMGP KVTQYWTEGP
     AADLAEQRLG HTMPVRRMFG QHMSVFPTCS FLPAINTIRT WHPRGPNEIE VWAFTLVDAD
     APAEIKEEYR RHNIRTFSAG GVFEQDDGEN WVEIQKGLRG YKAKSQPLNA QMGLGRSQTG
     HPDFPGNVGY VYAEEAARGM YHHWMRMMSE PSWATLKP