Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

3-hydroxyanthranilate 3,4-dioxygenase 1

Gene

bna1-1

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501DioxygenUniRule annotation
Metal bindingi54 – 541Iron; catalyticUniRule annotation
Metal bindingi60 – 601Iron; catalyticUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Metal bindingi102 – 1021Iron; catalyticUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation
Metal bindingi131 – 1311Divalent metal cationUniRule annotation
Metal bindingi134 – 1341Divalent metal cationUniRule annotation
Metal bindingi168 – 1681Divalent metal cationUniRule annotation
Metal bindingi171 – 1711Divalent metal cationUniRule annotation

GO - Molecular functioni

  1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB-HAMAP
  2. ferrous iron binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
  4. tryptophan catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase 1UniRule annotation (EC:1.13.11.6UniRule annotation)
Alternative name(s):
3-hydroxyanthranilate oxygenase 1UniRule annotation
Short name:
3-HAO-1UniRule annotation
3-hydroxyanthranilic acid dioxygenase 1UniRule annotation
Short name:
HAD-1UniRule annotation
Biosynthesis of nicotinic acid protein 1-1UniRule annotation
Gene namesi
Name:bna1-1
ORF Names:AO090023000314
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 3

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1921923-hydroxyanthranilate 3,4-dioxygenase 1PRO_0000361981Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00007302.

Structurei

3D structure databases

ProteinModelPortaliQ2UHT9.
SMRiQ2UHT9. Positions 5-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG7QK0Q0.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q2UHT9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPPALNIPK WLEANSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR
60 70 80 90 100
TDYHINTTPE FFYQYRGSML LRTVDTSASP PVFQDIPIHE GSLFLLPANT
110 120 130 140 150
PHCPVRFKDT VGVVMEQPRA EGAVDILRWY CKSCGEIVWE KRFVCTDLGT
160 170 180 190
QVKEVVEEFG ADQEKRTCKA CGTVAETKYK EGELVQPPRF LE
Length:192
Mass (Da):21,548
Last modified:January 23, 2006 - v1
Checksum:i2C34952C73846DEA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007157 Genomic DNA. Translation: BAE58876.1.
RefSeqiXP_001820878.1. XM_001820826.2.

Genome annotation databases

EnsemblFungiiCADAORAT00007452; CADAORAP00007302; CADAORAG00007452.
GeneIDi5992880.
KEGGiaor:AOR_1_538144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007157 Genomic DNA. Translation: BAE58876.1.
RefSeqiXP_001820878.1. XM_001820826.2.

3D structure databases

ProteinModelPortaliQ2UHT9.
SMRiQ2UHT9. Positions 5-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00007302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00007452; CADAORAP00007302; CADAORAG00007452.
GeneIDi5992880.
KEGGiaor:AOR_1_538144.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
KOiK00452.
OMAiKPPVGNQ.
OrthoDBiEOG7QK0Q0.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.

Family and domain databases

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

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry namei3HAO1_ASPOR
AccessioniPrimary (citable) accession number: Q2UHT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2009
Last sequence update: January 23, 2006
Last modified: January 6, 2015
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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

External Data

Dasty 3

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 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.