BPHA3_PSES1
ID BPHA3_PSES1 Reviewed; 109 AA.
AC Q52440;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Biphenyl dioxygenase ferredoxin subunit;
GN Name=bphA3;
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 -!- FUNCTION: This protein seems to be a 2Fe-2S ferredoxin.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (BphA1 and BphA2), a ferredoxin
CC (BphA3) and a ferredoxin reductase (BphA4).
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000305}.
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DR EMBL; D17319; BAA04139.1; -; Genomic_DNA.
DR PIR; JC2440; JC2440.
DR PDB; 2E4P; X-ray; 2.00 A; A/B=1-109.
DR PDB; 2E4Q; X-ray; 1.80 A; A/C=1-109.
DR PDB; 2YVJ; X-ray; 1.90 A; B=1-109.
DR PDBsum; 2E4P; -.
DR PDBsum; 2E4Q; -.
DR PDBsum; 2YVJ; -.
DR AlphaFoldDB; Q52440; -.
DR SMR; Q52440; -.
DR EvolutionaryTrace; Q52440; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Electron transport;
KW Iron; Iron-sulfur; Metal-binding; Transport.
FT CHAIN 1..109
FT /note="Biphenyl dioxygenase ferredoxin subunit"
FT /id="PRO_0000201687"
FT DOMAIN 4..100
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 63
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 66
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2E4Q"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:2E4Q"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2E4Q"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:2YVJ"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2E4Q"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2E4Q"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2E4Q"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2YVJ"
SQ SEQUENCE 109 AA; 11913 MW; 0D3BBB8C60C01751 CRC64;
MTFTKACSVD EVPPGEALQV SHDAQKVAIF NVDGEFFATQ DQCTHGEWSL SEGGYLDGDV
VECSLHMGKF CVRTGKVKSP PPCEPLKVYP IRIEGRDVLV DFSRAALHA
