ANDAB_BURCE
ID ANDAB_BURCE Reviewed; 108 AA.
AC Q84BZ1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Anthranilate 1,2-dioxygenase ferredoxin subunit {ECO:0000303|PubMed:13129960};
GN Name=andAb {ECO:0000312|EMBL:AAO83641.1};
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:AAO83641.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC 29424 / DBO1 {ECO:0000312|EMBL:AAO83641.1};
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. This protein seems to be a 2Fe-2S
CC ferredoxin. {ECO:0000269|PubMed:13129960, ECO:0000303|PubMed:13129960}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P0A185,
CC ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P0A185, 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: Expression is positively regulated by the transcriptional
CC regulator AndR. {ECO:0000269|PubMed:13129960}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin component family. {ECO:0000255}.
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DR EMBL; AY223539; AAO83641.1; -; Genomic_DNA.
DR AlphaFoldDB; Q84BZ1; -.
DR SMR; Q84BZ1; -.
DR STRING; 292.DM42_4274; -.
DR KEGG; ag:AAO83641; -.
DR eggNOG; COG2146; Bacteria.
DR BioCyc; MetaCyc:MON-7527; -.
DR UniPathway; UPA01016; UER01026.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043421; P:anthranilate catabolic process; IDA:CACAO.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Transport.
FT CHAIN 1..108
FT /note="Anthranilate 1,2-dioxygenase ferredoxin subunit"
FT /id="PRO_0000415161"
FT DOMAIN 9..105
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 51
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 71
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 108 AA; 11748 MW; F04D8BA295443D45 CRC64;
MTEATLAEWH PLGAIDEFTE DEPAARVAGQ KPIAVFRIGD ELFAMHDLCS HGHARLSEGY
VEDGCVECPL HQGLIDIRTG APKCAPITEP VRVYPIRIVD GQVEVNVG
