BPHA1_PSES1
ID BPHA1_PSES1 Reviewed; 458 AA.
AC Q52438;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Biphenyl dioxygenase subunit alpha;
DE EC=1.14.12.18;
DE AltName: Full=Biphenyl 2,3-dioxygenase;
GN Name=bphA1;
OS Pseudomonas sp. (strain KKS102).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=307;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8048958; DOI=10.1006/bbrc.1994.2008;
RA Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H.,
RA Takagi M., Yano K.;
RT "Identification of the bphA and bphB genes of Pseudomonas sp. strains
RT KKS102 involved in degradation of biphenyl and polychlorinated biphenyls.";
RL Biochem. Biophys. Res. Commun. 202:850-856(1994).
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 3 BphA1 subunits and 3 BphA2
CC subunits. A ferredoxin (BphA3) and a ferredoxin reductase (BphA4) must
CC be present to obtain activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D17319; BAA04137.1; -; Genomic_DNA.
DR PIR; JC2467; JC2467.
DR AlphaFoldDB; Q52438; -.
DR SMR; Q52438; -.
DR BRENDA; 1.14.12.18; 5085.
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_0000085049"
FT DOMAIN 59..157
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 103
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 121
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 124
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
SQ SEQUENCE 458 AA; 51876 MW; 128E8C38E2A3CFAA CRC64;
MGIYSEREVQ AVPMTFKRRW TDEAIRALVD QDKGLIDPRI YADQDLYEIE LERIFARSWL
LLGHEAHIPK TGDYLTTYMG EDPVIMVRQK DGSIKVFLNQ CRHRGMRICR SDAGNAKAFT
CTYHGWAYDI AGNLVNVPYE KEAFCDKKEG DCGFDKADWG PLQARVETYK GLIFANWDAE
APDLKTYLSD AMPYMDVMLD RTEAGTTVVG GMQKWVIPCN WKFAAEQFCS DMYHAGTMAH
LSGVLSSLPP EMDLTQVQMS KNGSQFRAAW GGHGSGWFIN DAAILMAVMG PKITQYWTQG
PAAEKAAKRL NQMPTQTMFG QHMTVFPTCS FLPGINTIRS WHPRGPNEVE CGPSWSSMPM
RPEDIKEEFR RQNIRTFNAG GTFEQDDGEN WVEIQRGLRG HKAKSAPLCA QMGLNVPNKS
NPDFPGKTAY VYAEEAARGM YHHWARMMSE PNWETLKP
