ANDAC_BURCE
ID ANDAC_BURCE Reviewed; 423 AA.
AC Q84BZ3;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Anthranilate 1,2-dioxygenase large subunit {ECO:0000303|PubMed:13129960};
DE EC=1.14.12.1 {ECO:0000269|PubMed:13129960};
GN Name=andAc {ECO:0000312|EMBL:AAO83639.1};
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:AAO83639.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBUNIT, AND INDUCTION.
RC STRAIN=ATCC 29424 / DBO1 {ECO:0000312|EMBL:AAO83639.1};
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:O85673};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:O85673};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:O85673,
CC ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:O85673, ECO:0000255|PROSITE-ProRule:PRU00628};
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 alpha subunit family. {ECO:0000255}.
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DR EMBL; AY223539; AAO83639.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84BZ3; -.
DR SMR; Q84BZ3; -.
DR STRING; 292.DM42_4276; -.
DR KEGG; ag:AAO83639; -.
DR eggNOG; COG4638; Bacteria.
DR BioCyc; MetaCyc:MON-7528; -.
DR BRENDA; 1.14.12.1; 1028.
DR UniPathway; UPA01016; UER01026.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018618; F:anthranilate 1,2-dioxygenase (deaminating, decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08880; RHO_alpha_C_ahdA1c-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043264; AhdA1c-like_alpha_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Dioxygenase; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase.
FT CHAIN 1..423
FT /note="Anthranilate 1,2-dioxygenase large subunit"
FT /id="PRO_0000415163"
FT DOMAIN 53..168
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 95
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 97
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 115
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 118
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P0A110,
FT ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 370
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
SQ SEQUENCE 423 AA; 48049 MW; 4F8A79384C5F6A97 CRC64;
MEQTASPVVF AARDDASDVH FPHDDGSRVP YKVFSSRAVY DREQERIFRG PTWNFVALEA
EIPNAGDFKS TFVGDTPVVV TRTEDGALSA WVNRCAHRGA QVCRKSRGNA SSHTCVYHQW
SFDNEGNLLG VPFRRGQKGM TGMPADFDPK QHGLRKLRVD SYRGLVFATF SDDVAPLPDY
LGAQMRPWID RIFHKPIEYL GCTRQYSKSN WKLYMENVKD PYHASMLHLF HTTFNIFRVG
MKARSIPDAN HGLHSIITVT KTGDDTSAAY KQQNIRSFDE GFHLEDESIL DLVSEYDEDC
TNHIQPIFPQ LVIQQIHNTL VARQILPKGP DNFELIFHFF GYADDTPELR ALRIKQANLV
GPAGYISMED TEATELVQRG TVRDADATSV IEMSRGNPEQ QDTVITESLI RKFWVGYQKL
MGY
