Q7SDX3 (3HAO_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-hydroxyanthranilate 3,4-dioxygenase
EC=1.13.11.6

Alternative name(s):
3-hydroxyanthranilate oxygenase
Short name=3-HAO
3-hydroxyanthranilic acid dioxygenase
Short name=HAD
Biosynthesis of nicotinic acid protein 1

Gene names

Name:	bna-1
ORF Names:	NCU03282

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate By similarity.
Catalytic activity	3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.
Cofactor	Fe2+ ion By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the 3-HAO family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-hydroxyanthranilate 3,4-dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 180	180	3-hydroxyanthranilate 3,4-dioxygenase		PRO_0000361991
Sites
	Metal binding	48	1	Iron; catalytic By similarity
	Metal binding	54	1	Iron; catalytic By similarity
	Metal binding	92	1	Iron; catalytic By similarity
	Metal binding	121	1	Divalent metal cation By similarity
	Metal binding	124	1	Divalent metal cation By similarity
	Metal binding	158	1	Divalent metal cation By similarity
	Metal binding	161	1	Divalent metal cation By similarity
	Binding site	44	1	Dioxygen By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7SDX3 [UniParc]. Last modified December 15, 2003. Version 1. Checksum: 932C6A2C709B50DE	FASTA	180	20,557
	10 20 30 40 50 60 MLSSPVNLPK WLEENSHLLK PPINNYCVYN DDFTVMIVGG PNARTDYHIN QTPEWFYQYK 70 80 90 100 110 120 GAMMLKVVDD GNFRDIIIRE GEMFLLPGNT PHNPVRFADT VGIVLEQKRP ADTIDRMRWY 130 140 150 160 170 180 CQNCKEIVHE ASFHCTDLGT QIKAAVEAFK GNEQLRTCKK CGVLADWSPK PGSIQDPNVQ

References

[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: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABX02000009 Genomic DNA. Translation: EAA34972.1.
RefSeq	XP_964208.1. XM_959115.2.
UniGene	Ncr.16733.
3D structure databases
HSSP	HSSP built from PDB template 1ZVF based on UniProtKB P47096.
ProteinModelPortal	Q7SDX3.
SMR	Q7SDX3. Positions 3-170.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7SDX3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	EFNCRT00000002760; EFNCRP00000002760; EFNCRG00000002757.
GeneID	3880357.
KEGG	ncr:NCU03282.
NMPDR	fig|5141.1.peg.8651.
Phylogenomic databases
eggNOG	fuNOG08759.
GeneTree	EFGT00050000005674.
OMA	LKPPVNN.
OrthoDB	EOG476P8N.
Family and domain databases
InterPro	IPR010329. 3hydroanth_dOase. IPR011051. Cupin_RmlC_type. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KO	K00452.
PANTHER	PTHR15497. PTHR15497. 1 hit.
Pfam	PF06052. 3-HAO. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR03037. Anthran_nbaC. 1 hit.
ProtoNet	Search...

Entry information

Entry name

3HAO_NEUCR

Accession

Primary (citable) accession number: Q7SDX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	December 15, 2003
Last modified:	December 14, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program