ID   BNZD_PSEPU              Reviewed;         409 AA.
AC   P08087;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component;
DE            EC=1.18.1.3;
DE   AltName: Full=P4 subunit;
GN   Name=bnzD;
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).
CC   -!- FUNCTION: Part of the electron transfer component of benzene 1,2-
CC       dioxygenase, transfers electrons from ferredoxin (BnzC) to NADH.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADH + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:16521, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.18.1.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
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 reductase family. {ECO:0000305}.
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DR   EMBL; M17904; AAA25738.1; -; Genomic_DNA.
DR   AlphaFoldDB; P08087; -.
DR   SMR; P08087; -.
DR   UniPathway; UPA00272; UER00391.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
DR   SUPFAM; SSF55424; SSF55424; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..409
FT                   /note="Benzene 1,2-dioxygenase system ferredoxin--NAD(+)
FT                   reductase component"
FT                   /id="PRO_0000167651"
FT   BINDING         4..35
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         145..173
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   409 AA;  42820 MW;  20451B8A657FB895 CRC64;
     MATHVAIIGN GVGGFTTAQA LRAEGFEGRI SLIGDEPHLP YDRPSLSKAV LDGSLERPPI
     LAEADWYGEA RIDMLTGPEV TALDVQTRTI SLDDGTTLSA DAIVIATGSR ARTMALPGSQ
     LPGVVTLRTY GDVQVLRDSW TSATRLLIVG GGLIGCEVAT TARKLGLSVT ILEAGDELLV
     RVLGRRIGAW LRGLLTELGV QVELGTGVVG FSGEGQLEQV MASDGRSFVA DSALICVGAE
     PADQLARQAG LACDRGVIVD HCGATLAKGY SPSEMWPVGA AAGGRRSLET YMNAQRQAAA
     VAAAILGKNV SAPQLPVSWT EIAGHRMQMA GDIEGPGDFV SRGMPGSGAA LLFRLQERRI
     QAVVAVDAPR DFALATRLVE ARAAIEPARL ADLSNSMRDF VRANEGDLT