BPHF_PARXL
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 03-AUG-2022, entry version 127.
DE RecName: Full=Biphenyl dioxygenase system ferredoxin subunit;
GN Name=bphF; OrderedLocusNames=Bxeno_C1128; ORFNames=Bxe_C1194;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC 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}.
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DR EMBL; M86348; AAB63428.1; -; Genomic_DNA.
DR EMBL; CP000272; ABE37056.1; -; Genomic_DNA.
DR PIR; E41858; E41858.
DR RefSeq; WP_011494297.1; NZ_CP008761.1.
DR PDB; 1FQT; X-ray; 1.60 A; A/B=1-109.
DR PDBsum; 1FQT; -.
DR AlphaFoldDB; P37332; -.
DR SMR; P37332; -.
DR STRING; 266265.Bxe_C1194; -.
DR EnsemblBacteria; ABE37056; ABE37056; Bxe_C1194.
DR KEGG; bxb:DR64_8611; -.
DR KEGG; bxe:Bxe_C1194; -.
DR eggNOG; COG2146; Bacteria.
DR OMA; VECSLHM; -.
DR EvolutionaryTrace; P37332; -.
DR Proteomes; UP000001817; Chromosome 3.
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; 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 STRAND 49..51
FT /evidence="ECO:0007829|PDB:1FQT"
FT STRAND 60..62
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 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
