ID   ANDAA_BURCE             Reviewed;         406 AA.
AC   Q84BZ0;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Anthranilate 1,2-dioxygenase system ferredoxin--NAD(+) reductase component;
DE            EC=1.18.1.3;
GN   Name=andAa {ECO:0000312|EMBL:AAO83642.1};
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAO83642.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, SUBUNIT, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 29424 / DBO1 {ECO:0000312|EMBL:AAO83642.1};
RX   PubMed=13129960; DOI=10.1128/jb.185.19.5871-5881.2003;
RA   Chang H.K., Mohseni P., Zylstra G.J.;
RT   "Characterization and regulation of the genes for a novel anthranilate 1,2-
RT   dioxygenase from Burkholderia cepacia DBO1.";
RL   J. Bacteriol. 185:5871-5881(2003).
CC   -!- FUNCTION: Part of the multicomponent anthranilate dioxygenase, that
CC       converts anthranilate to catechol. Probably transfers electrons from
CC       ferredoxin (AndAb) to NADH. {ECO:0000269|PubMed:13129960}.
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         Evidence={ECO:0000250|UniProtKB:P43494};
CC   -!- PATHWAY: Aromatic compound metabolism; anthranilate degradation via
CC       hydroxylation; catechol from anthranilate: step 1/1.
CC       {ECO:0000269|PubMed:13129960}.
CC   -!- SUBUNIT: Part of a multicomponent enzyme system composed of a reductase
CC       (AndAa), a ferredoxin (AndAb) and a two-subunit oxygenase component
CC       (AndAc and AndAd). {ECO:0000269|PubMed:13129960}.
CC   -!- INDUCTION: Expression is positively regulated by the transcriptional
CC       regulator AndR. {ECO:0000269|PubMed:13129960}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC       anthranilate. {ECO:0000269|PubMed:13129960}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000255}.
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DR   EMBL; AY223539; AAO83642.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84BZ0; -.
DR   SMR; Q84BZ0; -.
DR   KEGG; ag:AAO83642; -.
DR   BioCyc; MetaCyc:MON-7526; -.
DR   UniPathway; UPA01016; UER01026.
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; FAD; Flavoprotein; NAD; Oxidoreductase.
FT   CHAIN           1..406
FT                   /note="Anthranilate 1,2-dioxygenase system ferredoxin--
FT                   NAD(+) reductase component"
FT                   /id="PRO_0000415160"
FT   BINDING         5..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P43494, ECO:0000255"
FT   BINDING         152..161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P16640, ECO:0000255"
SQ   SEQUENCE   406 AA;  42869 MW;  6FFD73C3218AA443 CRC64;
     MSADPFVIVG AGHAARRTAE ALRARDADAP IVMIGAEREL PYDRPALSKD ALLNDDGEQR
     AFVRDAAWYD AQRIALRLGT RVDAIEREAQ RVRLDDGTTL PYAKLVLATG SRVRTFGGPI
     DAGVVAHYVR TVADARALRA QLVRGRRVAV LGGGFIGLEV AAAARQLGCN VTVIDPAARL
     LQRALPEVVG AYAHRLHDER GVGFQMATLP RAIRAAAGGG AIVETDRGDV HADVVVVGIG
     VLPNVELAQA AGLDVDNGIR VDAGCRTADR AIFAAGEVTM HFNPLLGRHV RIESWQVAEN
     QPAVAAANLL GADDAYAELP WLWSDQYDCN LQMLGLFGAG QTTVVRGDPA RGPFTVFGLG
     GDGRIVAAAA VNLGRDIGAA RRLIAAGAMP DPQQLADPTV GLKTFL