ANTDA_ACIAD
ID ANTDA_ACIAD Reviewed; 471 AA.
AC O85673;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Anthranilate 1,2-dioxygenase large subunit {ECO:0000303|PubMed:11114907};
DE EC=1.14.12.1 {ECO:0000269|PubMed:11114907};
GN Name=antA {ECO:0000312|EMBL:AAC34813.1}; OrderedLocusNames=ACIAD2669;
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:AAC34813.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
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:CAG69424.1}
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, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, SUBUNIT, AND MUTAGENESIS OF MET-43.
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).
RN [4] {ECO:0000305}
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-217.
RX PubMed=14622009; DOI=10.1021/bi035385n;
RA Beharry Z.M., Eby D.M., Coulter E.D., Viswanathan R., Neidle E.L.,
RA Phillips R.S., Kurtz D.M. Jr.;
RT "Histidine ligand protonation and redox potential in the Rieske
RT dioxygenases: role of a conserved aspartate in anthranilate 1,2-
RT dioxygenase.";
RL Biochemistry 42:13625-13636(2003).
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:11114907};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:11114907};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628,
CC ECO:0000269|PubMed:11114907};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628, ECO:0000269|PubMed:11114907};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1 uM for anthranilate {ECO:0000269|PubMed:11114907,
CC ECO:0000269|PubMed:14622009};
CC KM=12 uM for benzoate {ECO:0000269|PubMed:11114907,
CC ECO:0000269|PubMed:14622009};
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, ECO:0000269|PubMed:14622009};
CC Redox potential:
CC E(0) is -86 +/-10 mV for Rieske center at pH 7.0.
CC {ECO:0000269|PubMed:11114907, ECO:0000269|PubMed:14622009};
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 -!- INDUCTION: By anthranilate. {ECO:0000269|PubMed:9721284}.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF071556; AAC34813.1; -; Genomic_DNA.
DR EMBL; CR543861; CAG69424.1; -; Genomic_DNA.
DR RefSeq; WP_004928945.1; NC_005966.1.
DR AlphaFoldDB; O85673; -.
DR SMR; O85673; -.
DR STRING; 62977.ACIAD2669; -.
DR PRIDE; O85673; -.
DR EnsemblBacteria; CAG69424; CAG69424; ACIAD2669.
DR GeneID; 45234944; -.
DR KEGG; aci:ACIAD2669; -.
DR eggNOG; COG4638; Bacteria.
DR HOGENOM; CLU_026244_4_1_6; -.
DR OMA; AQVGYNE; -.
DR OrthoDB; 275867at2; -.
DR BioCyc; ASP62977:ACIAD_RS12135-MON; -.
DR BioCyc; MetaCyc:MON-7505; -.
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: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 Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017638; Anthranilate_1-2-diOase_lsu.
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 TIGRFAMs; TIGR03228; anthran_1_2_A; 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; Reference proteome.
FT CHAIN 1..471
FT /note="Anthranilate 1,2-dioxygenase large subunit"
FT /id="PRO_0000415157"
FT DOMAIN 52..160
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 93
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 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 113
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 116
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 220
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P0A110"
FT MUTAGEN 43
FT /note="M->K: Prevents anthranilate degradation."
FT /evidence="ECO:0000269|PubMed:11114907"
FT MUTAGEN 217
FT /note="D->A: In ACN476; loss of dioxygenase activity and 2-
FT fold lower redox potential."
FT /evidence="ECO:0000269|PubMed:14622009"
FT MUTAGEN 217
FT /note="D->E: Loss of dioxygenase activity and lack of iron
FT at the mononuclear site."
FT /evidence="ECO:0000269|PubMed:14622009"
FT MUTAGEN 217
FT /note="D->N: Loss of dioxygenase activity."
FT /evidence="ECO:0000269|PubMed:14622009"
SQ SEQUENCE 471 AA; 53936 MW; 2DB8F0BA56CBED4A CRC64;
MTARNLAEWQ NFVQGCIDFR PNDGVYRIAR DMFTEPELFE LEMELIFEKV WIYACHESEI
PNNNDFVTVQ IGRQPMIVSR DGKGELHAMV NACEHRGATL TRVAKGNQSV FTCPFHAWCY
KSDGRLVKVK APGEYCEDFD KSSRGLKQGR IASYRGFVFV SLDTQATDSL EDFLGDAKVF
LDLMVDQSPT GELEVLQGKS AYTFAGNWKL QNENGLDGYH VSTVHYNYVS TVQHRQQVNA
AKGDELDTLD YSKLGAGDSE TDDGWFSFKN GHSVLFSDMP NPTVRPGYNT VMPYLVEKFG
EKRAEWAMHR LRNLNLYPSL FFMDQISSQL RIIRPVAWNK TEVISQCIGV KGESSEARRN
RIRQFEDFFN VSGLGTPDDL VEFREQQKGF QGRIERWSDI SRGYHQWTYG PTQNSQDLGI
EPVITGREFT HEGLYVNQHG QWQRLILDGL NKKALKMHDV TFDNQSVMDE V
