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P46952

- 3HAO_HUMAN

UniProt

P46952 - 3HAO_HUMAN

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

HAAO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.1 PublicationUniRule annotation

    Catalytic activityi

    3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.1 PublicationUniRule annotation

    Cofactori

    Fe2+ ion.1 PublicationUniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei43 – 431DioxygenUniRule annotation
    Metal bindingi47 – 471Iron; catalyticUniRule annotation
    Metal bindingi53 – 531Iron; catalyticUniRule annotation
    Binding sitei53 – 531SubstrateUniRule annotation
    Metal bindingi91 – 911Iron; catalyticUniRule annotation
    Binding sitei95 – 951SubstrateUniRule annotation
    Binding sitei105 – 1051SubstrateUniRule annotation

    GO - Molecular functioni

    1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB
    2. electron carrier activity Source: UniProtKB
    3. ferrous iron binding Source: UniProtKB
    4. oxygen binding Source: Ensembl

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    2. anthranilate metabolic process Source: UniProtKB-HAMAP
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. neuron cellular homeostasis Source: UniProtKB
    5. quinolinate biosynthetic process Source: UniProtKB
    6. response to cadmium ion Source: UniProtKB
    7. response to zinc ion Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. tryptophan catabolic process Source: Reactome

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08749-MONOMER.
    ReactomeiREACT_916. Tryptophan catabolism.
    UniPathwayiUPA00253; UER00330.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenaseUniRule annotation (EC:1.13.11.6UniRule annotation)
    Alternative name(s):
    3-hydroxyanthranilate oxygenaseUniRule annotation
    Short name:
    3-HAOUniRule annotation
    3-hydroxyanthranilic acid dioxygenaseUniRule annotation
    Short name:
    HADUniRule annotation
    Gene namesi
    Name:HAAOUniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4796. HAAO.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29171.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2862863-hydroxyanthranilate 3,4-dioxygenasePRO_0000064372Add
    BLAST

    Proteomic databases

    MaxQBiP46952.
    PaxDbiP46952.
    PRIDEiP46952.

    PTM databases

    PhosphoSiteiP46952.

    Expressioni

    Gene expression databases

    ArrayExpressiP46952.
    BgeeiP46952.
    CleanExiHS_HAAO.
    GenevestigatoriP46952.

    Organism-specific databases

    HPAiHPA036394.

    Interactioni

    Subunit structurei

    Monomer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi117047. 5 interactions.
    IntActiP46952. 2 interactions.
    MINTiMINT-1468803.
    STRINGi9606.ENSP00000294973.

    Structurei

    Secondary structure

    1
    286
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi7 – 137
    Helixi15 – 173
    Turni20 – 223
    Beta strandi24 – 3714
    Beta strandi46 – 483
    Beta strandi53 – 608
    Beta strandi62 – 687
    Beta strandi71 – 777
    Beta strandi81 – 855
    Beta strandi91 – 955
    Beta strandi100 – 1067
    Beta strandi114 – 1207
    Beta strandi123 – 13210
    Helixi137 – 14913
    Helixi152 – 1565
    Helixi161 – 1633
    Helixi183 – 1897
    Helixi191 – 1955
    Beta strandi200 – 2034
    Beta strandi207 – 2148
    Beta strandi216 – 2216
    Beta strandi228 – 2358
    Beta strandi237 – 2415
    Beta strandi244 – 2485
    Beta strandi252 – 2565
    Beta strandi262 – 2665
    Beta strandi271 – 2777
    Helixi279 – 2813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QNKX-ray1.60A2-286[»]
    ProteinModelPortaliP46952.
    SMRiP46952. Positions 2-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46952.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 160160Domain A (catalytic)UniRule annotationAdd
    BLAST
    Regioni161 – 17717LinkerUniRule annotationAdd
    BLAST
    Regioni178 – 286109Domain BUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG77058.
    HOGENOMiHOG000218448.
    HOVERGENiHBG000018.
    InParanoidiP46952.
    KOiK00452.
    OMAiFYCKDLG.
    OrthoDBiEOG7FFMS4.
    PhylomeDBiP46952.
    TreeFamiTF300246.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    HAMAPiMF_00825. 3_HAO.
    InterProiIPR010329. 3hydroanth_dOase.
    IPR016700. 3hydroanth_dOase_met.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR15497. PTHR15497. 1 hit.
    PfamiPF06052. 3-HAO. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
    SUPFAMiSSF51182. SSF51182. 2 hits.
    TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P46952-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERRLGVRAW VKENRGSFQP PVCNKLMHQE QLKVMFIGGP NTRKDYHIEE    50
    GEEVFYQLEG DMVLRVLEQG KHRDVVIRQG EIFLLPARVP HSPQRFANTV 100
    GLVVERRRLE TELDGLRYYV GDTMDVLFEK WFYCKDLGTQ LAPIIQEFFS 150
    SEQYRTGKPI PDQLLKEPPF PLSTRSIMEP MSLDAWLDSH HRELQAGTPL 200
    SLFGDTYETQ VIAYGQGSSE GLRQNVDVWL WQLEGSSVVT MGGRRLSLAP 250
    DDSLLVLAGT SYAWERTQGS VALSVTQDPA CKKPLG 286
    Length:286
    Mass (Da):32,556
    Last modified:October 5, 2010 - v2
    Checksum:i4DA6AC20FC6EC885
    GO
    Isoform 2 (identifier: P46952-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         148-286: Missing.

    Show »
    Length:147
    Mass (Da):17,275
    Checksum:i3ABF821D6C31CE9E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371I → V.3 Publications
    Corresponds to variant rs3816183 [ dbSNP | Ensembl ].
    VAR_021507
    Natural varianti42 – 421T → S.
    Corresponds to variant rs3816182 [ dbSNP | Ensembl ].
    VAR_030470

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei148 – 286139Missing in isoform 2. 2 PublicationsVSP_036239Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29481 mRNA. Translation: CAA82618.1.
    CR457063 mRNA. Translation: CAG33344.1.
    CR624693 mRNA. No translation available.
    AK295693 mRNA. Translation: BAG58544.1.
    AC098824 Genomic DNA. Translation: AAY14701.1.
    CH471053 Genomic DNA. Translation: EAX00309.1.
    BC029510 mRNA. Translation: AAH29510.1.
    CCDSiCCDS33187.1. [P46952-1]
    PIRiA54070.
    RefSeqiNP_036337.2. NM_012205.2. [P46952-1]
    UniGeneiHs.368805.

    Genome annotation databases

    EnsembliENST00000294973; ENSP00000294973; ENSG00000162882. [P46952-1]
    GeneIDi23498.
    KEGGihsa:23498.
    UCSCiuc002rst.4. human. [P46952-1]

    Polymorphism databases

    DMDMi308153402.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z29481 mRNA. Translation: CAA82618.1 .
    CR457063 mRNA. Translation: CAG33344.1 .
    CR624693 mRNA. No translation available.
    AK295693 mRNA. Translation: BAG58544.1 .
    AC098824 Genomic DNA. Translation: AAY14701.1 .
    CH471053 Genomic DNA. Translation: EAX00309.1 .
    BC029510 mRNA. Translation: AAH29510.1 .
    CCDSi CCDS33187.1. [P46952-1 ]
    PIRi A54070.
    RefSeqi NP_036337.2. NM_012205.2. [P46952-1 ]
    UniGenei Hs.368805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QNK X-ray 1.60 A 2-286 [» ]
    ProteinModelPortali P46952.
    SMRi P46952. Positions 2-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117047. 5 interactions.
    IntActi P46952. 2 interactions.
    MINTi MINT-1468803.
    STRINGi 9606.ENSP00000294973.

    PTM databases

    PhosphoSitei P46952.

    Polymorphism databases

    DMDMi 308153402.

    Proteomic databases

    MaxQBi P46952.
    PaxDbi P46952.
    PRIDEi P46952.

    Protocols and materials databases

    DNASUi 23498.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000294973 ; ENSP00000294973 ; ENSG00000162882 . [P46952-1 ]
    GeneIDi 23498.
    KEGGi hsa:23498.
    UCSCi uc002rst.4. human. [P46952-1 ]

    Organism-specific databases

    CTDi 23498.
    GeneCardsi GC02M042994.
    HGNCi HGNC:4796. HAAO.
    HPAi HPA036394.
    MIMi 604521. gene.
    neXtProti NX_P46952.
    PharmGKBi PA29171.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77058.
    HOGENOMi HOG000218448.
    HOVERGENi HBG000018.
    InParanoidi P46952.
    KOi K00452.
    OMAi FYCKDLG.
    OrthoDBi EOG7FFMS4.
    PhylomeDBi P46952.
    TreeFami TF300246.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00330 .
    BioCyci MetaCyc:HS08749-MONOMER.
    Reactomei REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSi HAAO. human.
    EvolutionaryTracei P46952.
    GenomeRNAii 23498.
    NextBioi 45867.
    PROi P46952.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46952.
    Bgeei P46952.
    CleanExi HS_HAAO.
    Genevestigatori P46952.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    HAMAPi MF_00825. 3_HAO.
    InterProi IPR010329. 3hydroanth_dOase.
    IPR016700. 3hydroanth_dOase_met.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR15497. PTHR15497. 1 hit.
    Pfami PF06052. 3-HAO. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017681. 3hydroanth_dOase_animal. 1 hit.
    SUPFAMi SSF51182. SSF51182. 2 hits.
    TIGRFAMsi TIGR03037. anthran_nbaC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase."
      Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., Lahm H., Cesura A.M.
      J. Biol. Chem. 269:13792-13797(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, VARIANT VAL-37.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-37.
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Hippocampus.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-37.
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    8. "Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase."
      Center for eukaryotic structural genomics (CESG)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NICKEL IONS.

    Entry informationi

    Entry namei3HAO_HUMAN
    AccessioniPrimary (citable) accession number: P46952
    Secondary accession number(s): A6NE56
    , B4DIN2, Q53QZ7, Q8N6N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3