ID   ANDAD_BURCE             Reviewed;         161 AA.
AC   Q84BZ2;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Anthranilate 1,2-dioxygenase small subunit {ECO:0000303|PubMed:13129960};
DE            EC=1.14.12.1 {ECO:0000269|PubMed:13129960};
GN   Name=andAd {ECO:0000312|EMBL:AAO83640.1};
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:AAO83640.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   SUBUNIT, AND INDUCTION.
RC   STRAIN=ATCC 29424 / DBO1 {ECO:0000312|EMBL:AAO83640.1};
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: Oxygenase component of anthranilate dioxygenase
CC       multicomponent enzyme system which catalyzes the incorporation of both
CC       atoms of molecular oxygen into anthranilate to form catechol. Can also
CC       act on benzoate and salicylate but not on 2-chlorobenzoate or o-
CC       toluate. {ECO:0000269|PubMed:13129960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anthranilate + 3 H(+) + NADH + O2 = catechol + CO2 + NAD(+) +
CC         NH4(+); Xref=Rhea:RHEA:11076, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16567, ChEBI:CHEBI:18135,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.14.12.1; Evidence={ECO:0000269|PubMed:13129960};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=anthranilate + 3 H(+) + NADPH + O2 = catechol + CO2 + NADP(+)
CC         + NH4(+); Xref=Rhea:RHEA:11072, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16567, ChEBI:CHEBI:18135,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.14.12.1; Evidence={ECO:0000269|PubMed:13129960};
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: By anthranilate but not by benzoate or salicylate.
CC       Expression is positively regulated by the transcriptional regulator
CC       AndR. {ECO:0000269|PubMed:13129960}.
CC   -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC       beta subunit family. {ECO:0000255}.
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DR   EMBL; AY223539; AAO83640.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84BZ2; -.
DR   SMR; Q84BZ2; -.
DR   STRING; 292.DM42_4275; -.
DR   KEGG; ag:AAO83640; -.
DR   eggNOG; COG5517; Bacteria.
DR   BioCyc; MetaCyc:MON-7530; -.
DR   BRENDA; 1.14.12.1; 1028.
DR   UniPathway; UPA01016; UER01026.
DR   GO; GO:0018618; F:anthranilate 1,2-dioxygenase (deaminating, decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   CDD; cd00667; ring_hydroxylating_dioxygenases_beta; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR   Pfam; PF00866; Ring_hydroxyl_B; 1.
DR   SUPFAM; SSF54427; SSF54427; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase.
FT   CHAIN           1..161
FT                   /note="Anthranilate 1,2-dioxygenase small subunit"
FT                   /id="PRO_0000415162"
SQ   SEQUENCE   161 AA;  18868 MW;  5496160C4714455F CRC64;
     MENLTEDMKT WFEIYMLQNR YIGHLDNDRL ERWPEMFTED CTYEIVPKEN ADLGLPVGIV
     HCTNQRMLRD RVVSLRHANI YEEHTYRHMT SGLAIVAQRD GEIDTESNYV VVQTRSNGES
     NVYQAGKYYD TVVRTPDGLR YKAKRVIYDT SRVQTLLATP I