BPHA_COMTE
ID BPHA_COMTE Reviewed; 457 AA.
AC Q46372;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Biphenyl dioxygenase subunit alpha;
DE EC=1.14.12.18;
DE AltName: Full=Biphenyl 2,3-dioxygenase;
GN Name=bphA;
OS Comamonas testosteroni (Pseudomonas testosteroni).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B-356;
RX PubMed=8890734; DOI=10.1016/0378-1119(96)00039-x;
RA Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D., Shareck F.,
RA Barriault D., Guillemette I., Juteau J.-M.;
RT "Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl
RT dioxygenase genes: evolutionary relationships among Gram-negative bacterial
RT biphenyl dioxygenases.";
RL Gene 174:195-202(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 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; U47637; AAC44526.1; -; Genomic_DNA.
DR PIR; JC4993; JC4993.
DR PDB; 3GZX; X-ray; 1.58 A; A=1-457.
DR PDB; 3GZY; X-ray; 1.62 A; A=1-457.
DR PDBsum; 3GZX; -.
DR PDBsum; 3GZY; -.
DR AlphaFoldDB; Q46372; -.
DR SMR; Q46372; -.
DR BRENDA; 1.14.12.18; 1590.
DR UniPathway; UPA00155; UER00250.
DR EvolutionaryTrace; Q46372; -.
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; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..457
FT /note="Biphenyl dioxygenase subunit alpha"
FT /id="PRO_0000085047"
FT DOMAIN 58..174
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:3GZX"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 232..239
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 282..297
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 300..308
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 348..357
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:3GZX"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:3GZX"
FT STRAND 423..431
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:3GZX"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:3GZX"
SQ SEQUENCE 457 AA; 51692 MW; D133FC0635FACBF5 CRC64;
MSSTMKDTQE APVRWSRNWT PDAIRALVDQ DNGKLDARIY ADQDLYQLEL ERVFGRSWLM
LGHETHIPKI GDYLTTYMGE DPVIMVRQKD QSIKVFLNQC RHRGMRIVRS DGGNAKAFTC
TYHGWAYDIA GNLVNVPFEK EAFCDKKEGD CGFDKADWGP LQARVETYKG LVFANWDPEA
PDLKTYLSDA MPYMDVMLDR TEAGTEAIGG IQKWVIPCNW KFAAEQFCSD MYHAGTMSHL
SGVLAGLPPE MDLTQIQLSK NGNQFRSAWG GHGAGWFIND SSILLSVVGP KITQYWTQGP
AAEKAARRVP QLPILDMFGQ HMTVFPTCSF LPGINTIRTW HPRGPNEVEV WAFVLVDADA
PEDIKEEFRL QNIRTFNAGG VFEQDDGENW VEIQRVMRGH KAKSTSLCAK MGLNVPNKNN
PAYPGKTAYV YAEEAARGMY HHWSRMMSEP SWDTLKP
