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
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
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 2 (bna5-2), Kynureninase 1 (bna5-1)
  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 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

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 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:AFUA_8G04650
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiFungiDB:Afu8g04650.

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 – 1921923-hydroxyanthranilate 3,4-dioxygenase 1PRO_0000361978Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ4WCF1.
SMRiQ4WCF1. Positions 5-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
InParanoidiQ4WCF1.
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.

Q4WCF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPPALNIPK WLEENSHLLQ PPVNNYCVYH PSSPATAGYT VMIVGGPNAR
60 70 80 90 100
TDYHINTTPE FFYQYRGSML LKTVDTSVSP PVFQDIPIHE GSIFLLPANT
110 120 130 140 150
PHCPVRFKDT VGVVMEQPRP KDAVDTMLWF CKKCGEVVWE KRFVCTDLGT
160 170 180 190
QVKEVVEEFA ADQEKRTCKA CGTIAETRYQ EGEVVQPPRF LE
Length:192
Mass (Da):21,705
Last modified:July 5, 2005 - v1
Checksum:i148D406C365727F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85233.1.
RefSeqiXP_747271.1. XM_742178.1.

Genome annotation databases

EnsemblFungiiCADAFUAT00003260; CADAFUAP00003260; CADAFUAG00003260.
GeneIDi3504643.
KEGGiafm:AFUA_8G04650.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAHF01000013 Genomic DNA. Translation: EAL85233.1.
RefSeqiXP_747271.1. XM_742178.1.

3D structure databases

ProteinModelPortaliQ4WCF1.
SMRiQ4WCF1. Positions 5-180.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAFUAT00003260; CADAFUAP00003260; CADAFUAG00003260.
GeneIDi3504643.
KEGGiafm:AFUA_8G04650.

Organism-specific databases

EuPathDBiFungiDB:Afu8g04650.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
InParanoidiQ4WCF1.
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. "Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
    Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.
    , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
    Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Entry informationi

Entry namei3HAO1_ASPFU
AccessioniPrimary (citable) accession number: Q4WCF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: July 5, 2005
Last modified: June 24, 2015
This is version 80 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.