ANTDC_ACIAD
ID ANTDC_ACIAD Reviewed; 343 AA.
AC O85675;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Anthranilate 1,2-dioxygenase electron transfer component {ECO:0000303|PubMed:11114907};
DE Includes:
DE RecName: Full=Ferredoxin {ECO:0000250|UniProtKB:Q51603};
DE Includes:
DE RecName: Full=Ferredoxin--NAD(+) reductase {ECO:0000250|UniProtKB:Q51603};
DE EC=1.18.1.3 {ECO:0000269|PubMed:11114907, ECO:0000312|EMBL:CAG69426.1};
GN Name=antC {ECO:0000312|EMBL:AAC34815.1}; OrderedLocusNames=ACIAD2671;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1] {ECO:0000312|EMBL:AAC34815.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=9721284; DOI=10.1128/jb.180.17.4466-4474.1998;
RA Bundy B.M., Campbell A.L., Neidle E.L.;
RT "Similarities between the antABC-encoded anthranilate dioxygenase and the
RT benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1.";
RL J. Bacteriol. 180:4466-4474(1998).
RN [2] {ECO:0000312|EMBL:CAG69426.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=11114907; DOI=10.1128/jb.183-1.109-118.2001;
RA Eby D.M., Beharry Z.M., Coulter E.D., Kurtz D.M. Jr., Neidle E.L.;
RT "Characterization and evolution of anthranilate 1,2-dioxygenase from
RT Acinetobacter sp. strain ADP1.";
RL J. Bacteriol. 183:109-118(2001).
CC -!- FUNCTION: Electron transfer component of anthranilate 1,2-dioxygenase
CC system. {ECO:0000269|PubMed:11114907}.
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 Evidence={ECO:0000269|PubMed:11114907};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11114907};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:11114907};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:11114907};
CC -!- PATHWAY: Aromatic compound metabolism; anthranilate degradation via
CC hydroxylation; catechol from anthranilate: step 1/1.
CC {ECO:0000269|PubMed:11114907}.
CC -!- SUBUNIT: Monomer. It is part of the anthranilate dioxygenase two
CC component enzyme system. The other component is an oxygenase component
CC consisting of 3 large (AntA) and 3 small (AntB) subunits.
CC {ECO:0000269|PubMed:11114907}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC ferredoxin reductase family. {ECO:0000255}.
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DR EMBL; AF071556; AAC34815.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG69426.1; -; Genomic_DNA.
DR AlphaFoldDB; O85675; -.
DR SMR; O85675; -.
DR STRING; 62977.ACIAD2671; -.
DR PRIDE; O85675; -.
DR EnsemblBacteria; CAG69426; CAG69426; ACIAD2671.
DR KEGG; aci:ACIAD2671; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR OMA; TCMGRCE; -.
DR OrthoDB; 1834577at2; -.
DR BioCyc; ASP62977:ACIAD_RS12145-MON; -.
DR BioCyc; MetaCyc:MON-7504; -.
DR UniPathway; UPA01016; UER01026.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..343
FT /note="Anthranilate 1,2-dioxygenase electron transfer
FT component"
FT /id="PRO_0000415159"
FT DOMAIN 3..96
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 103..206
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 98..338
FT /note="Ferredoxin-reductase"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 45
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 80
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 343 AA; 38549 MW; A8CEE4658B41234A CRC64;
MNHSVALNFA DGKTFFIAVQ EDELLLDAAV RQGINLPLDC REGVCGTCQG TCETGIYEQE
YVDEDALSER DLAKRKMLAC QTRVKSNAAF YFDHHSSICN AGETLKIATV VTGVELVSET
TAILHLDASQ HVKQLDFLPG QYARLQIPDT DDWRSYSFAN RPNASNQLQF LIRLLPNGVM
SNYLRERCQV GQTLIMEAPL GSFYLREVER PLVFIAGGTG LSAFLGMLDN IAEQPNQPSV
HLYYGVNTEA DLCEQKRLTT YAERIKNFSY HPIISKASEQ WQGKSGFIHE HLDKNQLSEQ
SFDMYLCGPP PMIEAVKTWL DEQAIADCHI YSEKFLQSNT AKT
