BNZC_PSEPU
ID BNZC_PSEPU Reviewed; 107 AA.
AC P08086;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Benzene 1,2-dioxygenase system ferredoxin subunit;
DE AltName: Full=P3 subunit;
GN Name=bnzC;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BE-81;
RX PubMed=3667527; DOI=10.1128/jb.169.11.5174-5179.1987;
RA Irie S., Doi S., Yorifuji T., Takagi M., Yano K.;
RT "Nucleotide sequencing and characterization of the genes encoding benzene
RT oxidation enzymes of Pseudomonas putida.";
RL J. Bacteriol. 169:5174-5179(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-107.
RC STRAIN=ML2;
RX PubMed=3360142; DOI=10.1016/0014-5793(88)80845-7;
RA Morrice N., Geary P., Cammack R., Harris A., Beg F., Aitken A.;
RT "Primary structure of protein B from Pseudomonas putida, member of a new
RT class of 2Fe-2S ferredoxins.";
RL FEBS Lett. 231:336-340(1988).
CC -!- FUNCTION: This protein seems to be a 2Fe-2S ferredoxin.
CC -!- PATHWAY: Aromatic compound metabolism; benzene degradation; catechol
CC from benzene: step 1/2.
CC -!- SUBUNIT: This dioxygenase system consists of four proteins: the two
CC subunits of the hydroxylase component (BnzA and BnzB), a ferredoxin
CC (BnzC) and a ferredoxin reductase (BnzD).
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; M17904; AAA25737.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P08086; -.
DR SMR; P08086; -.
DR UniPathway; UPA00272; UER00391.
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; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Metal-binding; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3360142"
FT CHAIN 2..107
FT /note="Benzene 1,2-dioxygenase system ferredoxin subunit"
FT /id="PRO_0000201685"
FT DOMAIN 4..99
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 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT VARIANT 24
FT /note="P -> S (in strain: ML2)"
FT VARIANT 52
FT /note="D -> E (in strain: ML2)"
FT VARIANT 59
FT /note="I -> V (in strain: ML2)"
FT VARIANT 88
FT /note="F -> Y (in strain: ML2)"
FT VARIANT 92
FT /note="V -> I (in strain: ML2)"
SQ SEQUENCE 107 AA; 11906 MW; 48E78CF78C4D1B5D CRC64;
MTWTYILRQS DLPPGEMQRY EGGPEPVMVC NVDGDFFAVQ DTCTHGDWAL SDGYLDGDIV
ECTLHFGKFC VRTGKVKALP ACKPIKVFPI KVEGDEVHVD LDNGELK