ID BPHF_PARXL Reviewed; 109 AA. AC P37332; Q13FT3; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 02-SEP-2026, entry version 141. DE RecName: Full=Biphenyl dioxygenase system ferredoxin subunit; GN Name=bphF; OrderedLocusNames=Bxeno_C1128; ORFNames=Bxe_C1194; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; 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 SEQUENCE REVISION. RA Erickson B.D., Mondello F.J.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] RP CHARACTERIZATION. RX PubMed=11141059; DOI=10.1021/bi001780r; RA Couture M.M.-J., Colbert C.L., Babini E., Rosell F.I., Mauk A.G., RA Bolin J.T., Eltis L.D.; RT "Characterization of BphF, a Rieske-type ferredoxin with a low reduction RT potential."; RL Biochemistry 40:84-92(2001). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=11188691; DOI=10.1016/s0969-2126(00)00536-0; RA Colbert C.L., Couture M.M.-J., Eltis L.D., Bolin J.T.; RT "A cluster exposed: structure of the Rieske ferredoxin from biphenyl RT dioxygenase and the redox properties of Rieske Fe-S proteins."; RL Structure 8:1267-1278(2000). CC -!- FUNCTION: This protein seems to be a 2Fe-2S ferredoxin. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -157 mV.; CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two CC subunits of the hydroxylase component (BphA and BphE), a ferredoxin CC (BphF) and a ferredoxin reductase (BphG). CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase CC ferredoxin component 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; M86348; AAB63428.1; -; Genomic_DNA. DR EMBL; CP000272; ABE37056.1; -; Genomic_DNA. DR PIR; E41858; E41858. DR RefSeq; WP_011494297.1; NC_007953.1. DR PDB; 1FQT; X-ray; 1.60 A; A/B=1-109. DR AlphaFoldDB; P37332; -. DR SMR; P37332; -. DR STRING; 266265.Bxe_C1194; -. DR KEGG; bxb:DR64_8611; -. DR KEGG; bxe:Bxe_C1194; -. DR eggNOG; COG2146; Bacteria. DR OrthoDB; 9800167at2; -. DR EvolutionaryTrace; P37332; -. DR Proteomes; UP000001817; Chromosome 3. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR CDD; cd03528; Rieske_RO_ferredoxin; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR InterPro; IPR017941; Rieske_2Fe-2S. DR InterPro; IPR036922; Rieske_2Fe-2S_sf. DR PANTHER; PTHR21496:SF23; 3-PHENYLPROPIONATE_CINNAMIC ACID DIOXYGENASE FERREDOXIN SUBUNIT; 1. DR PANTHER; PTHR21496; FERREDOXIN-RELATED; 1. DR Pfam; PF00355; Rieske; 1. DR SUPFAM; SSF50022; ISP domain; 1. DR PROSITE; PS51296; RIESKE; 1. DR PDBsum; 1FQT; -. PE 1: Evidence at protein level; KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Electron transport; KW Iron; Iron-sulfur; Metal-binding; Reference proteome; Transport. FT CHAIN 1..109 FT /note="Biphenyl dioxygenase system ferredoxin subunit" FT /id="PRO_0000201686" 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 BINDING 45 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 63 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT BINDING 66 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT STRAND 4..8 FT /evidence="ECO:0007829|PDB:1FQT" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 25..32 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:1FQT" FT TURN 50..52 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 53..57 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:1FQT" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1FQT" FT TURN 72..74 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:1FQT" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:1FQT" FT STRAND 97..100 FT /evidence="ECO:0007829|PDB:1FQT" SQ SEQUENCE 109 AA; 11955 MW; 39AE9C8B84232FA4 CRC64; MKFTRVCDRR DVPEGEALKV ESGGTSVAIF NVDGELFATQ DRCTHGDWSL SDGGYLEGDV VECSLHMGKF CVRTGKVKSP PPCEALKIFP IRIEDNDVLV DFEAGYLAP //