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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

Haao

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Fe2+UniRule annotation

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Kynurenine 3-monooxygenase (Kmo)
  2. Kynureninase (Kynu)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (Haao), 3-hydroxyanthranilate 3,4-dioxygenase (Haao)
This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei43DioxygenUniRule annotation1
Metal bindingi47Iron; catalyticUniRule annotation1
Metal bindingi53Iron; catalyticUniRule annotation1
Binding sitei53SubstrateUniRule annotation1
Metal bindingi91Iron; catalyticUniRule annotation1
Binding sitei95SubstrateUniRule annotation1
Binding sitei105SubstrateUniRule annotation1

GO - Molecular functioni

  • 3-hydroxyanthranilate 3,4-dioxygenase activity Source: RGD
  • iron ion binding Source: RGD
  • oxygen binding Source: RGD

GO - Biological processi

  • NAD biosynthetic process Source: UniProtKB-UniPathway
  • quinolinate metabolic process Source: RGD

Keywordsi

Molecular functionDioxygenase, Oxidoreductase
Biological processPyridine nucleotide biosynthesis
LigandIron, Metal-binding

Enzyme and pathway databases

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:Haao
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71071. Haao.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: RGD
  • mitochondrial membrane Source: RGD

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3108658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000643741 – 2863-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST286

Proteomic databases

PaxDbiP46953.
PRIDEiP46953.

PTM databases

iPTMnetiP46953.
PhosphoSitePlusiP46953.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

MINTiMINT-4569623.
STRINGi10116.ENSRNOP00000043835.

Chemistry databases

BindingDBiP46953.

Structurei

3D structure databases

ProteinModelPortaliP46953.
SMRiP46953.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 160Domain A (catalytic)UniRule annotationAdd BLAST160
Regioni161 – 177LinkerUniRule annotationAdd BLAST17
Regioni178 – 286Domain BUniRule annotationAdd BLAST109

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiKOG3995. Eukaryota.
ENOG4111GH8. LUCA.
HOGENOMiHOG000218448.
HOVERGENiHBG000018.
InParanoidiP46953.
KOiK00452.
PhylomeDBiP46953.
TreeFamiTF300246.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
HAMAPiMF_00825. 3_HAO. 1 hit.
InterProiView protein in InterPro
IPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiView protein in Pfam
PF06052. 3-HAO. 1 hit.
PIRSFiPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMiSSF51182. SSF51182. 2 hits.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

Sequencei

Sequence statusi: Complete.

P46953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERCVRVKSW VEENRASFQP PVCNKLMHRE QLKIMFVGGP NTRKDYHIEE
60 70 80 90 100
GEEVFYQLEG DMVLRVLEQG EHRDVVIRQG EIFLLPARVP HSPQRFANTM
110 120 130 140 150
GLVIERRRME TELDGLRYYV GDTEDVLFEK WFHCKDLGTQ LAPIIQEFFH
160 170 180 190 200
SEQYRTGKPN PDQLLKEPPF PLSTRSVMEP MSLKAWLESH SRELQAGTSL
210 220 230 240 250
SLFGDSYETQ VIAHGQGSSK GPRQDVDVWL WQLEGSSKVT MGGQCVALAP
260 270 280
DDSLLVPAGF SYMWERAQGS VALSVTQDPA CKKPLG
Length:286
Mass (Da):32,582
Last modified:December 15, 1998 - v2
Checksum:iB4F535AD8949DAB7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti29R → Q in AAH85739 (PubMed:15489334).Curated1
Sequence conflicti44K → S AA sequence (PubMed:7514594).Curated1
Sequence conflicti199S → F AA sequence (PubMed:7514594).Curated1
Sequence conflicti204G → C AA sequence (PubMed:7514594).Curated1
Sequence conflicti214H → Y AA sequence (PubMed:7514594).Curated1
Sequence conflicti229W → P AA sequence (PubMed:7514594).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D44494 mRNA. Translation: BAA07937.1.
BC085739 mRNA. Translation: AAH85739.1.
D28339 mRNA. Translation: BAA21019.1.
RefSeqiNP_064461.1. NM_020076.2.
UniGeneiRn.48675.

Genome annotation databases

GeneIDi56823.
KEGGirno:56823.
UCSCiRGD:71071. rat.

Similar proteinsi

Entry informationi

Entry namei3HAO_RAT
AccessioniPrimary (citable) accession number: P46953
Secondary accession number(s): P70474, Q5RKK0, Q64556
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 15, 1998
Last modified: August 30, 2017
This is version 130 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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