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Protein

Anthranilate 1,2-dioxygenase large subunit

Gene

antA

Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of anthranilate dioxygenase multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into anthranilate to form catechol.1 Publication

Catalytic activityi

Anthranilate + NAD(P)H + O2 = catechol + CO2 + NAD(P)+ + NH3.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Fe cation1 PublicationNote: Binds 1 Fe cation per subunit.1 Publication
  • [2Fe-2S] clusterPROSITE-ProRule annotation1 PublicationNote: Binds 1 [2Fe-2S] cluster per subunit.PROSITE-ProRule annotation1 Publication

Redox potential

E0 is -86 +/-10 mV for Rieske center at pH 7.0.2 Publications

Kineticsi

KM values measured using the AntAB complex.

  1. KM=1 µM for anthranilate2 Publications
  2. KM=12 µM for benzoate2 Publications

    pH dependencei

    Optimum pH is 6.3 for the reverse reaction.2 Publications

    Pathwayi: anthranilate degradation via hydroxylation

    This protein is involved in step 1 of the subpathway that synthesizes catechol from anthranilate.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Anthranilate 1,2-dioxygenase electron transfer component (antC), Anthranilate 1,2-dioxygenase large subunit (antA), Anthranilate 1,2-dioxygenase small subunit (antB)
    This subpathway is part of the pathway anthranilate degradation via hydroxylation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes catechol from anthranilate, the pathway anthranilate degradation via hydroxylation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi93 – 931Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity
    Metal bindingi95 – 951Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity
    Metal bindingi113 – 1131Iron-sulfur (2Fe-2S)PROSITE-ProRule annotationBy similarity
    Metal bindingi116 – 1161Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotationBy similarity
    Metal bindingi220 – 2201IronBy similarity
    Metal bindingi225 – 2251IronBy similarity
    Metal bindingi379 – 3791IronBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

    Enzyme and pathway databases

    BioCyciASP62977:GJVV-2483-MONOMER.
    MetaCyc:MONOMER-7505.
    UniPathwayiUPA01016; UER01026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate 1,2-dioxygenase large subunit1 Publication (EC:1.14.12.11 Publication)
    Gene namesi
    Name:antAImported
    Ordered Locus Names:ACIAD2669
    OrganismiAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
    Taxonomic identifieri62977 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter
    Proteomesi
    • UP000000430 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431M → K: Prevents anthranilate degradation. 1 Publication
    Mutagenesisi217 – 2171D → A in ACN476; loss of dioxygenase activity and 2-fold lower redox potential. 1 Publication
    Mutagenesisi217 – 2171D → E: Loss of dioxygenase activity and lack of iron at the mononuclear site. 1 Publication
    Mutagenesisi217 – 2171D → N: Loss of dioxygenase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 471471Anthranilate 1,2-dioxygenase large subunitPRO_0000415157Add
    BLAST

    Expressioni

    Inductioni

    By anthranilate.1 Publication

    Interactioni

    Subunit structurei

    The anthranilate dioxygenase (AntDO) multicomponent enzyme system is composed of an oxygenase component and a NADH:acceptor reductase component (AntC). The oxygenase component is a heterohexamer of 3 large (AntA) and 3 small (AntB) subunits.1 Publication

    Protein-protein interaction databases

    STRINGi62977.ACIAD2669.

    Structurei

    3D structure databases

    ProteinModelPortaliO85673.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 160109RieskePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Rieske domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG4108Q89. Bacteria.
    COG4638. LUCA.
    HOGENOMiHOG000140938.
    KOiK05599.
    OMAiAWNKTEI.
    OrthoDBiEOG6W19DT.

    Family and domain databases

    Gene3Di2.102.10.10. 1 hit.
    3.90.380.10. 1 hit.
    InterProiIPR017638. Anthranilate_1-2-diOase_lsu.
    IPR017941. Rieske_2Fe-2S.
    IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
    IPR015879. Ring_hydroxy_dOase_asu_C_dom.
    IPR001663. Rng_hydr_dOase-A.
    [Graphical view]
    PfamiPF00355. Rieske. 1 hit.
    PF00848. Ring_hydroxyl_A. 1 hit.
    [Graphical view]
    PRINTSiPR00090. RNGDIOXGNASE.
    SUPFAMiSSF50022. SSF50022. 1 hit.
    TIGRFAMsiTIGR03228. anthran_1_2_A. 1 hit.
    PROSITEiPS51296. RIESKE. 1 hit.
    PS00570. RING_HYDROXYL_ALPHA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O85673-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTARNLAEWQ NFVQGCIDFR PNDGVYRIAR DMFTEPELFE LEMELIFEKV
    60 70 80 90 100
    WIYACHESEI PNNNDFVTVQ IGRQPMIVSR DGKGELHAMV NACEHRGATL
    110 120 130 140 150
    TRVAKGNQSV FTCPFHAWCY KSDGRLVKVK APGEYCEDFD KSSRGLKQGR
    160 170 180 190 200
    IASYRGFVFV SLDTQATDSL EDFLGDAKVF LDLMVDQSPT GELEVLQGKS
    210 220 230 240 250
    AYTFAGNWKL QNENGLDGYH VSTVHYNYVS TVQHRQQVNA AKGDELDTLD
    260 270 280 290 300
    YSKLGAGDSE TDDGWFSFKN GHSVLFSDMP NPTVRPGYNT VMPYLVEKFG
    310 320 330 340 350
    EKRAEWAMHR LRNLNLYPSL FFMDQISSQL RIIRPVAWNK TEVISQCIGV
    360 370 380 390 400
    KGESSEARRN RIRQFEDFFN VSGLGTPDDL VEFREQQKGF QGRIERWSDI
    410 420 430 440 450
    SRGYHQWTYG PTQNSQDLGI EPVITGREFT HEGLYVNQHG QWQRLILDGL
    460 470
    NKKALKMHDV TFDNQSVMDE V
    Length:471
    Mass (Da):53,936
    Last modified:November 1, 1998 - v1
    Checksum:i2DB8F0BA56CBED4A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF071556 Genomic DNA. Translation: AAC34813.1.
    CR543861 Genomic DNA. Translation: CAG69424.1.
    RefSeqiWP_004928945.1. NC_005966.1.

    Genome annotation databases

    EnsemblBacteriaiCAG69424; CAG69424; ACIAD2669.
    GeneIDi25685157.
    KEGGiaci:ACIAD2669.
    PATRICi20742937. VBIAciSp98416_2409.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF071556 Genomic DNA. Translation: AAC34813.1.
    CR543861 Genomic DNA. Translation: CAG69424.1.
    RefSeqiWP_004928945.1. NC_005966.1.

    3D structure databases

    ProteinModelPortaliO85673.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi62977.ACIAD2669.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAG69424; CAG69424; ACIAD2669.
    GeneIDi25685157.
    KEGGiaci:ACIAD2669.
    PATRICi20742937. VBIAciSp98416_2409.

    Phylogenomic databases

    eggNOGiENOG4108Q89. Bacteria.
    COG4638. LUCA.
    HOGENOMiHOG000140938.
    KOiK05599.
    OMAiAWNKTEI.
    OrthoDBiEOG6W19DT.

    Enzyme and pathway databases

    UniPathwayiUPA01016; UER01026.
    BioCyciASP62977:GJVV-2483-MONOMER.
    MetaCyc:MONOMER-7505.

    Family and domain databases

    Gene3Di2.102.10.10. 1 hit.
    3.90.380.10. 1 hit.
    InterProiIPR017638. Anthranilate_1-2-diOase_lsu.
    IPR017941. Rieske_2Fe-2S.
    IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
    IPR015879. Ring_hydroxy_dOase_asu_C_dom.
    IPR001663. Rng_hydr_dOase-A.
    [Graphical view]
    PfamiPF00355. Rieske. 1 hit.
    PF00848. Ring_hydroxyl_A. 1 hit.
    [Graphical view]
    PRINTSiPR00090. RNGDIOXGNASE.
    SUPFAMiSSF50022. SSF50022. 1 hit.
    TIGRFAMsiTIGR03228. anthran_1_2_A. 1 hit.
    PROSITEiPS51296. RIESKE. 1 hit.
    PS00570. RING_HYDROXYL_ALPHA. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1."
      Bundy B.M., Campbell A.L., Neidle E.L.
      J. Bacteriol. 180:4466-4474(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      Strain: ATCC 33305 / BD413 / ADP1.
    2. "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
      Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
      Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 33305 / BD413 / ADP1.
    3. "Characterization and evolution of anthranilate 1,2-dioxygenase from Acinetobacter sp. strain ADP1."
      Eby D.M., Beharry Z.M., Coulter E.D., Kurtz D.M. Jr., Neidle E.L.
      J. Bacteriol. 183:109-118(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, MUTAGENESIS OF MET-43.
      Strain: ATCC 33305 / BD413 / ADP1.
    4. "Histidine ligand protonation and redox potential in the Rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase."
      Beharry Z.M., Eby D.M., Coulter E.D., Viswanathan R., Neidle E.L., Phillips R.S., Kurtz D.M. Jr.
      Biochemistry 42:13625-13636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-217.

    Entry informationi

    Entry nameiANTDA_ACIAD
    AccessioniPrimary (citable) accession number: O85673
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: November 1, 1998
    Last modified: November 11, 2015
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.