ID   BEDA_PSEPU              Reviewed;         410 AA.
AC   Q07946;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit;
DE            EC=1.18.1.3;
GN   Name=bedA;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OG   Plasmid pHMT112.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 3-14.
RC   STRAIN=ML2;
RX   PubMed=8344526; DOI=10.1016/0378-1119(93)90343-2;
RA   Tan H.-M., Tang H.-Y., Joannou C., Abdel-Wahab N.H., Mason J.R.;
RT   "The Pseudomonas putida ML2 plasmid-encoded genes for benzene dioxygenase
RT   are unusual in codon usage and low in G+C content.";
RL   Gene 130:33-39(1993).
CC   -!- FUNCTION: Part of the electron transfer component of benzene 1,2-
CC       dioxygenase, transfers electrons from ferredoxin 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 (BedC1 and BedC2), a ferredoxin
CC       (BedB) and a ferredoxin reductase (BedA).
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       ferredoxin reductase family. {ECO:0000305}.
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DR   EMBL; AF148496; AAA17761.1; -; Genomic_DNA.
DR   PIR; JN0810; JN0810.
DR   AlphaFoldDB; Q07946; -.
DR   SMR; Q07946; -.
DR   BioCyc; MetaCyc:MON-12882; -.
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   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW   Flavoprotein; NAD; Oxidoreductase; Plasmid.
FT   CHAIN           1..410
FT                   /note="Benzene 1,2-dioxygenase system ferredoxin--NAD(+)
FT                   reductase subunit"
FT                   /id="PRO_0000167652"
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   410 AA;  43587 MW;  1852467DC01D41EA CRC64;
     MANHVAIIGN GVAGFTTAQA LRAEGYEGRI SLIGEEQHLP YDRPSLSKAV LDGSFEQPPR
     LAEADWYSEA SIEMLTGSEV TDLDTQKKMI SLNDGSTISA DAIVIATGSR ARMLSLPGSQ
     LPGVVTLRTY GDVQLLRDSW TPNTRLLIVG GGLIGCEVAT TARKLGLSVT ILEAGDELLV
     RVLGRRIGAW LRGLLTEQGV QVELKTGVSG FSGEGQLEKV MVNDGRSFIA DNALICVGAD
     PADQLARQAG LECDRGVVVD HRGATSAKGI FAVGDVATWP LHSGGKRSLE TYMNAQRQAT
     AVAKAILGKE VSAPQLPVSW TEIAGHRMQM AGDIEGPGEY VLRGTLGIGS ALLFRLLDGR
     IQAVVAVDAP RDFALANRLV EAQVIIEPEK LADVSNNMRD IVRANEGNQK