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Protein

3-hydroxyanthranilate 3,4-dioxygenase 2

Gene

bna1-2

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

Pathway: 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 (bna4)
  2. Kynureninase 1 (bna5-1), Kynureninase 2 (bna5-2)
  3. 3-hydroxyanthranilate 3,4-dioxygenase 1 (bna1-1), 3-hydroxyanthranilate 3,4-dioxygenase 2 (bna1-2)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441DioxygenUniRule annotation
Metal bindingi48 – 481Iron; catalyticUniRule annotation
Metal bindingi60 – 601Iron; catalyticUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Metal bindingi99 – 991Iron; catalyticUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei113 – 1131SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

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 2UniRule annotation (EC:1.13.11.6UniRule annotation)
Alternative name(s):
3-hydroxyanthranilate oxygenase 2UniRule annotation
Short name:
3-HAO-2UniRule annotation
3-hydroxyanthranilic acid dioxygenase 2UniRule annotation
Short name:
HAD-2UniRule annotation
Biosynthesis of nicotinic acid protein 1-2UniRule annotation
Gene namesi
Name:bna1-2
ORF Names:AO090102000066
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564 Componenti: Chromosome 4

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1791793-hydroxyanthranilate 3,4-dioxygenase 2PRO_0000361982Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00009249.

Structurei

3D structure databases

ProteinModelPortaliQ2UB88.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
OMAiIREEAFH.
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.

Q2UB88-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPPFSFASW VAENEDKLHP PVNNYCLYSG EDFTLMVVGG PNSRNDYHGV
60 70 80 90 100
FIMVVNQTEE WFYQVKGDML LRIVENNTTF RDISIKEGEM FLLPGNTPHN
110 120 130 140 150
PVRFRDTIGL VMERKRPEDS LDRLRWYCSK GKHKKPTIIR EEIFHCADLG
160 170
TQLKPLIERW QIDEESRRCG ACGAIADPK
Length:179
Mass (Da):20,762
Last modified:January 24, 2006 - v1
Checksum:i4F9749F43A058800
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007162 Genomic DNA. Translation: BAE61177.1.

Genome annotation databases

EnsemblFungiiCADAORAT00009437; CADAORAP00009249; CADAORAG00009437.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007162 Genomic DNA. Translation: BAE61177.1.

3D structure databases

ProteinModelPortaliQ2UB88.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00009249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00009437; CADAORAP00009249; CADAORAG00009437.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
OMAiIREEAFH.
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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry namei3HAO2_ASPOR
AccessioniPrimary (citable) accession number: Q2UB88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: January 24, 2006
Last modified: January 7, 2015
This is version 70 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.