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Protein

Anthranilate 3-monooxygenase oxygenase component

Gene

hpaH

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Utilizes FADH2 supplied by NAD(P)H-dependent FAD/FMN reductase (GTNG_3158) to catalyze the hydroxylation of anthranilate producing 3-hydroxyanthranilate. Preferred substrate is anthranilate but it can also utilize 2-hydroxyphenylacetate, 4-hydroxyphenylacetate and salicylate but not kynurenine, phenol, 2-NBA, chlorobenzene, naphthalene, naphthol, toluene or ethylbenzene.1 Publication

Catalytic activityi

Anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O.1 Publication
4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H2O.By similarity1 Publication

Kineticsi

    1. Vmax=151.3 µmol/min/mg enzyme toward anthranilate1 Publication

    pH dependencei

    Optimum pH is 9.0. Active from pH 5 to 11.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius. Active from 25 to 70 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei151 – 1511SubstrateBy similarity
    Binding sitei194 – 1941FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi151 – 1533FADBy similarity
    Nucleotide bindingi157 – 1604FADBy similarity
    Nucleotide bindingi457 – 4604FADBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciGTHE420246:GIXT-3256-MONOMER.
    MetaCyc:MONOMER-15633.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anthranilate 3-monooxygenase oxygenase component1 PublicationBy similarity (EC:1.14.14.81 Publication)
    Alternative name(s):
    4-hydroxyphenylacetate 3-monooxygenase oxygenase componentBy similarity (EC:1.14.14.9By similarity)
    Short name:
    4 HPA 3-hydroxylaseBy similarity
    Anthranilate 3-hydroxylase1 PublicationBy similarity
    Anthranilate hydroxylase1 Publication
    Gene namesi
    Name:hpaHBy similarity
    Ordered Locus Names:GTNG_3160
    OrganismiGeobacillus thermodenitrificans (strain NG80-2)
    Taxonomic identifieri420246 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
    Proteomesi
    • UP000001578 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Anthranilate 3-monooxygenase oxygenase componentPRO_0000420234Add
    BLAST

    Interactioni

    Subunit structurei

    Anthranilate 3-monooxygenase consists of a reductase component (GTNG_3158) and an oxygenase component HpaH.

    Protein-protein interaction databases

    STRINGi420246.GTNG_3160.

    Structurei

    3D structure databases

    ProteinModelPortaliA4IT51.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni105 – 1095Substrate bindingBy similarity
    Regioni207 – 2082Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the FADH(2)-utilizing monooxygenase family.Sequence analysis

    Phylogenomic databases

    eggNOGiENOG4105EFA. Bacteria.
    COG2368. LUCA.
    HOGENOMiHOG000145842.
    KOiK16901.
    OMAiHAIINPQ.
    OrthoDBiEOG6P3337.

    Family and domain databases

    InterProiIPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    IPR004925. HpaB/PvcC/4-BUDH.
    IPR024719. HpaB/PvcC/4-BUDH_C.
    IPR024674. HpaB/PvcC/4-BUDH_N.
    [Graphical view]
    PfamiPF03241. HpaB. 1 hit.
    PF11794. HpaB_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000331. HpaA_HpaB. 1 hit.
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A4IT51-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRMGIRTGAQ YISGLKSRKP EIWLSGRRVI NVCEEPVFKQ PIREIARLYD
    60 70 80 90 100
    MQHDPEYQDK ITHICTETGE RVSNAFLVPK SREDLLARRA LFEVWARATF
    110 120 130 140 150
    GLMGRTPDFL NVVLTSLYSN ASFLEKYNPQ WAENIRAYYR YVRDNDLFLT
    160 170 180 190 200
    HAIINPQNDR SKPSHEQQDT FTHLGVVRET PEGLIVRGAK MLATLAPITD
    210 220 230 240 250
    EVIIYTFPGY KPGDERYAVS FAIPIDTPGL RILCREPMQD GTRPLFDHPL
    260 270 280 290 300
    ASRFEEMDAL LVFNDVLVPW DRVFIYNNVE AANLLYPKTG IAQQPAHQTG
    310 320 330 340 350
    VRGLIKLQFA TEVAIRLADS IGVDVYLNVQ NDLGELLQSV EAIRALLHLA
    360 370 380 390 400
    EHELEVLPSG EVMPGWVPLE TIRGLLPKLY PRAVEVLQII GAGGLLMSPT
    410 420 430 440 450
    GADFANPELA ADMEKYYAGR IGVGGEERVR LFKLAWDLCG EAFGQRLLQY
    460 470 480 490
    ERFYTGDPIR KRAIFYNNIK RERTLVMVDE ALRMPNQQEK VVNA
    Length:494
    Mass (Da):56,164
    Last modified:May 1, 2007 - v1
    Checksum:iDE503A3E68B96F86
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68505.1.

    Genome annotation databases

    EnsemblBacteriaiABO68505; ABO68505; GTNG_3160.
    KEGGigtn:GTNG_3160.
    PATRICi21982963. VBIGeoThe136879_3324.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68505.1.

    3D structure databases

    ProteinModelPortaliA4IT51.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi420246.GTNG_3160.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABO68505; ABO68505; GTNG_3160.
    KEGGigtn:GTNG_3160.
    PATRICi21982963. VBIGeoThe136879_3324.

    Phylogenomic databases

    eggNOGiENOG4105EFA. Bacteria.
    COG2368. LUCA.
    HOGENOMiHOG000145842.
    KOiK16901.
    OMAiHAIINPQ.
    OrthoDBiEOG6P3337.

    Enzyme and pathway databases

    BioCyciGTHE420246:GIXT-3256-MONOMER.
    MetaCyc:MONOMER-15633.

    Family and domain databases

    InterProiIPR009075. AcylCo_DH/oxidase_C.
    IPR009100. AcylCoA_DH/oxidase_NM_dom.
    IPR004925. HpaB/PvcC/4-BUDH.
    IPR024719. HpaB/PvcC/4-BUDH_C.
    IPR024674. HpaB/PvcC/4-BUDH_N.
    [Graphical view]
    PfamiPF03241. HpaB. 1 hit.
    PF11794. HpaB_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000331. HpaA_HpaB. 1 hit.
    SUPFAMiSSF47203. SSF47203. 1 hit.
    SSF56645. SSF56645. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
      Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
      Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NG80-2.
    2. "Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2."
      Liu X., Dong Y., Li X., Ren Y., Li Y., Wang W., Wang L., Feng L.
      Microbiology 156:589-595(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NG80-21 Publication.

    Entry informationi

    Entry nameiHPAH_GEOTN
    AccessioniPrimary (citable) accession number: A4IT51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: May 1, 2007
    Last modified: December 9, 2015
    This is version 57 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

    Documents

    1. 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.