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P46952 (3HAO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:HAAO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate. Ref.1

Catalytic activity

3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde. Ref.1

Cofactor

Fe2+ ion. Ref.1

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 3/3. HAMAP-Rule MF_03019

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_03019.

Sequence similarities

Belongs to the 3-HAO family.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandIron
Metal-binding
   Molecular functionDioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

neuron cellular homeostasis

Inferred from mutant phenotype PubMed 2967497. Source: UniProtKB

quinolinate biosynthetic process

Non-traceable author statement PubMed 12007609Ref.1. Source: UniProtKB

response to cadmium ion

Inferred from direct assay PubMed 12007609. Source: UniProtKB

response to zinc ion

Inferred from direct assay PubMed 12007609. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tryptophan catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrial membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_function3-hydroxyanthranilate 3,4-dioxygenase activity

Inferred from direct assay PubMed 12007609Ref.1. Source: UniProtKB

electron carrier activity

Non-traceable author statement Ref.1. Source: UniProtKB

ferrous iron binding

Inferred from direct assay PubMed 12007609. Source: UniProtKB

oxygen binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P46952-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P46952-2)

The sequence of this isoform differs from the canonical sequence as follows:
     148-286: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2862863-hydroxyanthranilate 3,4-dioxygenase HAMAP-Rule MF_03019
PRO_0000064372

Regions

Region1 – 160160Domain A (catalytic) By similarity
Region161 – 17717Linker By similarity
Region178 – 286109Domain B By similarity

Sites

Metal binding471Iron; catalytic By similarity
Metal binding531Iron; catalytic By similarity
Metal binding911Iron; catalytic By similarity
Binding site431Dioxygen By similarity
Binding site531Substrate By similarity
Binding site951Substrate By similarity
Binding site1051Substrate By similarity

Natural variations

Alternative sequence148 – 286139Missing in isoform 2.
VSP_036239
Natural variant371I → V. Ref.1 Ref.2 Ref.6
Corresponds to variant rs3816183 [ dbSNP | Ensembl ].
VAR_021507
Natural variant421T → S.
Corresponds to variant rs3816182 [ dbSNP | Ensembl ].
VAR_030470

Secondary structure

.......................................................... 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 4DA6AC20FC6EC885

FASTA28632,556
        10         20         30         40         50         60 
MERRLGVRAW VKENRGSFQP PVCNKLMHQE QLKVMFIGGP NTRKDYHIEE GEEVFYQLEG 

        70         80         90        100        110        120 
DMVLRVLEQG KHRDVVIRQG EIFLLPARVP HSPQRFANTV GLVVERRRLE TELDGLRYYV 

       130        140        150        160        170        180 
GDTMDVLFEK WFYCKDLGTQ LAPIIQEFFS SEQYRTGKPI PDQLLKEPPF PLSTRSIMEP 

       190        200        210        220        230        240 
MSLDAWLDSH HRELQAGTPL SLFGDTYETQ VIAYGQGSSE GLRQNVDVWL WQLEGSSVVT 

       250        260        270        280 
MGGRRLSLAP DDSLLVLAGT SYAWERTQGS VALSVTQDPA CKKPLG 

« Hide

Isoform 2 [UniParc].

Checksum: 3ABF821D6C31CE9E
Show »

FASTA14717,275

References

« Hide 'large scale' references
[1]"Molecular cloning and functional expression of human 3-hydroxyanthranilic-acid dioxygenase."
Malherbe P., Kohler C., da Prada M., Lang G., Kiefer V., Schwarcz R., Lahm H., Cesura A.M.
J. Biol. Chem. 269:13792-13797(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR, VARIANT VAL-37.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-37.
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hippocampus.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-37.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]"Crystal structure of human 3-hydroxyanthranilate 3,4-dioxygenase."
Center for eukaryotic structural genomics (CESG)
Submitted (AUG-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NICKEL IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29481 mRNA. Translation: CAA82618.1.
CR457063 mRNA. Translation: CAG33344.1.
CR624693 mRNA. No translation available.
AK295693 mRNA. Translation: BAG58544.1.
AC098824 Genomic DNA. Translation: AAY14701.1.
CH471053 Genomic DNA. Translation: EAX00309.1.
BC029510 mRNA. Translation: AAH29510.1.
PIRA54070.
RefSeqNP_036337.2. NM_012205.2.
UniGeneHs.368805.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QNKX-ray1.60A2-286[»]
ProteinModelPortalP46952.
SMRP46952. Positions 2-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117047. 5 interactions.
IntActP46952. 2 interactions.
MINTMINT-1468803.
STRING9606.ENSP00000294973.

PTM databases

PhosphoSiteP46952.

Polymorphism databases

DMDM308153402.

Proteomic databases

PaxDbP46952.
PRIDEP46952.

Protocols and materials databases

DNASU23498.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000294973; ENSP00000294973; ENSG00000162882. [P46952-1]
GeneID23498.
KEGGhsa:23498.
UCSCuc002rst.4. human. [P46952-1]

Organism-specific databases

CTD23498.
GeneCardsGC02M042994.
HGNCHGNC:4796. HAAO.
HPAHPA036394.
MIM604521. gene.
neXtProtNX_P46952.
PharmGKBPA29171.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG77058.
HOGENOMHOG000218448.
HOVERGENHBG000018.
InParanoidP46952.
KOK00452.
OMAFYCKDLG.
OrthoDBEOG7FFMS4.
PhylomeDBP46952.
TreeFamTF300246.

Enzyme and pathway databases

BioCycMetaCyc:HS08749-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00253; UER00330.

Gene expression databases

ArrayExpressP46952.
BgeeP46952.
CleanExHS_HAAO.
GenevestigatorP46952.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
HAMAPMF_00825. 3_HAO.
InterProIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMSSF51182. SSF51182. 2 hits.
TIGRFAMsTIGR03037. anthran_nbaC. 1 hit.
ProtoNetSearch...

Other

ChiTaRSHAAO. human.
EvolutionaryTraceP46952.
GenomeRNAi23498.
NextBio45867.
PROP46952.
SOURCESearch...

Entry information

Entry name3HAO_HUMAN
AccessionPrimary (citable) accession number: P46952
Secondary accession number(s): A6NE56 expand/collapse secondary AC list , B4DIN2, Q53QZ7, Q8N6N9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM