ANTDB_ACIAD
ID ANTDB_ACIAD Reviewed; 163 AA.
AC O85674;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Anthranilate 1,2-dioxygenase small subunit {ECO:0000303|PubMed:11114907};
DE EC=1.14.12.1 {ECO:0000269|PubMed:11114907};
GN Name=antB {ECO:0000312|EMBL:AAC34814.1}; OrderedLocusNames=ACIAD2670;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC34814.1}
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:CAG69425.1}
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, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP SUBUNIT.
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: Component of anthranilate dioxygenase multicomponent enzyme
CC system which catalyzes the incorporation of both atoms of molecular
CC oxygen into anthranilate to form catechol.
CC {ECO:0000269|PubMed:11114907}.
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:11114907};
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:11114907};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for anthranilate {ECO:0000269|PubMed:11114907};
CC KM=12 uM for benzoate {ECO:0000269|PubMed:11114907};
CC Note=KM values measured using the AntAB complex.;
CC pH dependence:
CC Optimum pH is 6.3 for the reverse reaction.
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: The anthranilate dioxygenase (AntDO) multicomponent enzyme
CC system is composed of an oxygenase component and a NADH:acceptor
CC reductase component (AntC). The oxygenase component is a heterohexamer
CC of 3 large (AntA) and 3 small (AntB) subunits.
CC {ECO:0000269|PubMed:11114907}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC beta subunit family. {ECO:0000255}.
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DR EMBL; AF071556; AAC34814.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG69425.1; -; Genomic_DNA.
DR RefSeq; WP_004928948.1; NC_005966.1.
DR AlphaFoldDB; O85674; -.
DR SMR; O85674; -.
DR STRING; 62977.ACIAD2670; -.
DR EnsemblBacteria; CAG69425; CAG69425; ACIAD2670.
DR GeneID; 45234945; -.
DR KEGG; aci:ACIAD2670; -.
DR eggNOG; COG5517; Bacteria.
DR HOGENOM; CLU_102527_0_1_6; -.
DR OMA; CDAQDWD; -.
DR OrthoDB; 1736098at2; -.
DR BioCyc; ASP62977:ACIAD_RS12140-MON; -.
DR BioCyc; MetaCyc:MON-7506; -.
DR UniPathway; UPA01016; UER01026.
DR Proteomes; UP000000430; Chromosome.
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; IPR017640; Anthranilate_1-2-diOase_ssu.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR000391; Rng_hydr_dOase-bsu.
DR PANTHER; PTHR41534; PTHR41534; 1.
DR Pfam; PF00866; Ring_hydroxyl_B; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR TIGRFAMs; TIGR03231; anthran_1_2_B; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Dioxygenase; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..163
FT /note="Anthranilate 1,2-dioxygenase small subunit"
FT /id="PRO_0000415158"
SQ SEQUENCE 163 AA; 19331 MW; F9B6F39D96EF7226 CRC64;
MSLELHFAVS QFLYKKAELC DNYDWDAYID LYDEDSEYHI PQWIDDHNYV QDPNQGLSYI
YYEDRSGLED RVFRIRTGKA ASATPLPRTQ HNIHNVQVKT LEDGLIEAKV SWRTLYNRQG
LEGCFYGRAT YVLRPTEDSF RIRRQHSVLL NDKIDSVLDF YHV
