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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

bna1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
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:iNAD(+) 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 (nic-3)
  2. Kynureninase 1 (kyn-1), Kynureninase 2 (kyn-2)
  3. 3-hydroxyanthranilate 3,4-dioxygenase (bna1)
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 bindingi54 – 541Iron; catalyticUniRule annotation
Binding sitei54 – 541SubstrateUniRule annotation
Metal bindingi92 – 921Iron; catalyticUniRule annotation
Binding sitei96 – 961SubstrateUniRule annotation
Binding sitei106 – 1061SubstrateUniRule annotation
Metal bindingi121 – 1211Divalent metal cationUniRule annotation
Metal bindingi124 – 1241Divalent metal cationUniRule annotation
Metal bindingi158 – 1581Divalent metal cationUniRule annotation
Metal bindingi161 – 1611Divalent 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-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
Biosynthesis of nicotinic acid protein 1UniRule annotation
Gene namesi
Name:bna1
ORF Names:NCU03282
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 1, Linkage Group I

Organism-specific databases

EuPathDBiFungiDB:NCU03282.

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 – 1801803-hydroxyanthranilate 3,4-dioxygenasePRO_0000361991Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ7SDX3.
SMRiQ7SDX3. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
InParanoidiQ7SDX3.
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.

Q7SDX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSPVNLPK WLEENSHLLK PPINNYCVYN DDFTVMIVGG PNARTDYHIN
60 70 80 90 100
QTPEWFYQYK GAMMLKVVDD GNFRDIIIRE GEMFLLPGNT PHNPVRFADT
110 120 130 140 150
VGIVLEQKRP ADTIDRMRWY CQNCKEIVHE ASFHCTDLGT QIKAAVEAFK
160 170 180
GNEQLRTCKK CGVLADWSPK PGSIQDPNVQ
Length:180
Mass (Da):20,557
Last modified:December 15, 2003 - v1
Checksum:i932C6A2C709B50DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002236 Genomic DNA. Translation: EAA34972.1.
RefSeqiXP_964208.1. XM_959115.3.

Genome annotation databases

EnsemblFungiiEFNCRT00000002760; EFNCRP00000002760; EFNCRG00000002757.
GeneIDi3880357.
KEGGincr:NCU03282.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM002236 Genomic DNA. Translation: EAA34972.1.
RefSeqiXP_964208.1. XM_959115.3.

3D structure databases

ProteinModelPortaliQ7SDX3.
SMRiQ7SDX3. Positions 3-170.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000002760; EFNCRP00000002760; EFNCRG00000002757.
GeneIDi3880357.
KEGGincr:NCU03282.

Organism-specific databases

EuPathDBiFungiDB:NCU03282.

Phylogenomic databases

eggNOGiNOG77058.
HOGENOMiHOG000218448.
InParanoidiQ7SDX3.
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. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry namei3HAO_NEUCR
AccessioniPrimary (citable) accession number: Q7SDX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: December 15, 2003
Last modified: July 22, 2015
This is version 86 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.