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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

HAAO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Fe2+1 PublicationUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431DioxygenUniRule annotation
Metal bindingi47 – 471Iron; catalyticUniRule annotation
Metal bindingi53 – 531Iron; catalyticUniRule annotation
Binding sitei53 – 531SubstrateUniRule annotation
Metal bindingi91 – 911Iron; catalyticUniRule annotation
Binding sitei95 – 951SubstrateUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation

GO - Molecular functioni

  1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB
  2. electron carrier activity Source: UniProtKB
  3. ferrous iron binding Source: UniProtKB
  4. oxygen binding Source: Ensembl

GO - Biological processi

  1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
  2. anthranilate metabolic process Source: UniProtKB-HAMAP
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. neuron cellular homeostasis Source: UniProtKB
  5. quinolinate biosynthetic process Source: UniProtKB
  6. response to cadmium ion Source: UniProtKB
  7. response to zinc ion Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
  9. tryptophan catabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08749-MONOMER.
ReactomeiREACT_916. Tryptophan catabolism.
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
Gene namesi
Name:HAAOUniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4796. HAAO.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29171.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2862863-hydroxyanthranilate 3,4-dioxygenasePRO_0000064372Add
BLAST

Proteomic databases

MaxQBiP46952.
PaxDbiP46952.
PRIDEiP46952.

PTM databases

PhosphoSiteiP46952.

Expressioni

Gene expression databases

BgeeiP46952.
CleanExiHS_HAAO.
ExpressionAtlasiP46952. baseline.
GenevestigatoriP46952.

Organism-specific databases

HPAiHPA036394.

Interactioni

Subunit structurei

Monomer.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi117047. 5 interactions.
IntActiP46952. 2 interactions.
MINTiMINT-1468803.
STRINGi9606.ENSP00000294973.

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi7 – 137Combined sources
Helixi15 – 173Combined sources
Turni20 – 223Combined sources
Beta strandi24 – 3714Combined sources
Beta strandi46 – 483Combined sources
Beta strandi53 – 608Combined sources
Beta strandi62 – 687Combined sources
Beta strandi71 – 777Combined sources
Beta strandi81 – 855Combined sources
Beta strandi91 – 955Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi123 – 13210Combined sources
Helixi137 – 14913Combined sources
Helixi152 – 1565Combined sources
Helixi161 – 1633Combined sources
Helixi183 – 1897Combined sources
Helixi191 – 1955Combined sources
Beta strandi200 – 2034Combined sources
Beta strandi207 – 2148Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi228 – 2358Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi252 – 2565Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi271 – 2777Combined sources
Helixi279 – 2813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QNKX-ray1.60A2-286[»]
ProteinModelPortaliP46952.
SMRiP46952. Positions 2-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46952.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 160160Domain A (catalytic)UniRule annotationAdd
BLAST
Regioni161 – 17717LinkerUniRule annotationAdd
BLAST
Regioni178 – 286109Domain BUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the 3-HAO family.UniRule annotation

Phylogenomic databases

eggNOGiNOG77058.
GeneTreeiENSGT00390000013008.
HOGENOMiHOG000218448.
HOVERGENiHBG000018.
InParanoidiP46952.
KOiK00452.
OMAiFYCKDLG.
OrthoDBiEOG7FFMS4.
PhylomeDBiP46952.
TreeFamiTF300246.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFiPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMiSSF51182. SSF51182. 2 hits.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P46952-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MERRLGVRAW VKENRGSFQP PVCNKLMHQE QLKVMFIGGP NTRKDYHIEE
60 70 80 90 100
GEEVFYQLEG DMVLRVLEQG KHRDVVIRQG EIFLLPARVP HSPQRFANTV
110 120 130 140 150
GLVVERRRLE TELDGLRYYV GDTMDVLFEK WFYCKDLGTQ LAPIIQEFFS
160 170 180 190 200
SEQYRTGKPI PDQLLKEPPF PLSTRSIMEP MSLDAWLDSH HRELQAGTPL
210 220 230 240 250
SLFGDTYETQ VIAYGQGSSE GLRQNVDVWL WQLEGSSVVT MGGRRLSLAP
260 270 280
DDSLLVLAGT SYAWERTQGS VALSVTQDPA CKKPLG
Length:286
Mass (Da):32,556
Last modified:October 5, 2010 - v2
Checksum:i4DA6AC20FC6EC885
GO
Isoform 2 (identifier: P46952-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:147
Mass (Da):17,275
Checksum:i3ABF821D6C31CE9E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371I → V.3 Publications
Corresponds to variant rs3816183 [ dbSNP | Ensembl ].
VAR_021507
Natural varianti42 – 421T → S.
Corresponds to variant rs3816182 [ dbSNP | Ensembl ].
VAR_030470

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei148 – 286139Missing in isoform 2. 2 PublicationsVSP_036239Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33187.1. [P46952-1]
PIRiA54070.
RefSeqiNP_036337.2. NM_012205.2. [P46952-1]
UniGeneiHs.368805.

Genome annotation databases

EnsembliENST00000294973; ENSP00000294973; ENSG00000162882. [P46952-1]
GeneIDi23498.
KEGGihsa:23498.
UCSCiuc002rst.4. human. [P46952-1]

Polymorphism databases

DMDMi308153402.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33187.1. [P46952-1]
PIRiA54070.
RefSeqiNP_036337.2. NM_012205.2. [P46952-1]
UniGeneiHs.368805.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QNKX-ray1.60A2-286[»]
ProteinModelPortaliP46952.
SMRiP46952. Positions 2-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117047. 5 interactions.
IntActiP46952. 2 interactions.
MINTiMINT-1468803.
STRINGi9606.ENSP00000294973.

Chemistry

BindingDBiP46952.
ChEMBLiCHEMBL3108657.

PTM databases

PhosphoSiteiP46952.

Polymorphism databases

DMDMi308153402.

Proteomic databases

MaxQBiP46952.
PaxDbiP46952.
PRIDEiP46952.

Protocols and materials databases

DNASUi23498.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294973; ENSP00000294973; ENSG00000162882. [P46952-1]
GeneIDi23498.
KEGGihsa:23498.
UCSCiuc002rst.4. human. [P46952-1]

Organism-specific databases

CTDi23498.
GeneCardsiGC02M042994.
HGNCiHGNC:4796. HAAO.
HPAiHPA036394.
MIMi604521. gene.
neXtProtiNX_P46952.
PharmGKBiPA29171.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG77058.
GeneTreeiENSGT00390000013008.
HOGENOMiHOG000218448.
HOVERGENiHBG000018.
InParanoidiP46952.
KOiK00452.
OMAiFYCKDLG.
OrthoDBiEOG7FFMS4.
PhylomeDBiP46952.
TreeFamiTF300246.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00330.
BioCyciMetaCyc:HS08749-MONOMER.
ReactomeiREACT_916. Tryptophan catabolism.

Miscellaneous databases

ChiTaRSiHAAO. human.
EvolutionaryTraceiP46952.
GenomeRNAii23498.
NextBioi45867.
PROiP46952.
SOURCEiSearch...

Gene expression databases

BgeeiP46952.
CleanExiHS_HAAO.
ExpressionAtlasiP46952. baseline.
GenevestigatoriP46952.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
HAMAPiMF_00825. 3_HAO.
InterProiIPR010329. 3hydroanth_dOase.
IPR016700. 3hydroanth_dOase_met.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR15497. PTHR15497. 1 hit.
PfamiPF06052. 3-HAO. 1 hit.
[Graphical view]
PIRSFiPIRSF017681. 3hydroanth_dOase_animal. 1 hit.
SUPFAMiSSF51182. SSF51182. 2 hits.
TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry namei3HAO_HUMAN
AccessioniPrimary (citable) accession number: P46952
Secondary accession number(s): A6NE56
, B4DIN2, Q53QZ7, Q8N6N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 5, 2010
Last modified: January 7, 2015
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.