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Protein

Dihydropteridine reductase

Gene

qdpr

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.By similarity

Catalytic activityi

A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 3025NADPBy similarityAdd
BLAST

GO - Molecular functioni

  • 6,7-dihydropteridine reductase activity Source: UniProtKB
  • NAD binding Source: dictyBase
  • protein homodimerization activity Source: dictyBase

GO - Biological processi

  • response to oxidative stress Source: dictyBase
  • tetrahydrobiopterin biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.5.1.34. 1939.
ReactomeiR-DDI-71182. Phenylalanine and tyrosine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydropteridine reductase (EC:1.5.1.34)
Alternative name(s):
Quinoid dihydropteridine reductase
Gene namesi
Name:qdpr
ORF Names:DDB_G0272684
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0272684. qdpr.

Subcellular locationi

GO - Cellular componenti

  • phagocytic vesicle Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Dihydropteridine reductasePRO_0000327797Add
BLAST

Proteomic databases

PaxDbiQ86A17.
PRIDEiQ86A17.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: dictyBase

Protein-protein interaction databases

MINTiMINT-8198634.
STRINGi44689.DDB0237752.

Structurei

Secondary structure

1
231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Turni9 – 113Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 358Combined sources
Beta strandi40 – 456Combined sources
Helixi51 – 6212Combined sources
Turni63 – 653Combined sources
Beta strandi68 – 736Combined sources
Helixi88 – 11326Combined sources
Beta strandi114 – 12310Combined sources
Helixi126 – 1294Combined sources
Helixi136 – 15217Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi164 – 1718Combined sources
Helixi176 – 1816Combined sources
Helixi187 – 1893Combined sources
Helixi193 – 20513Combined sources
Helixi207 – 2093Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi225 – 2306Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ORFX-ray2.16A/B/C/D1-231[»]
ProteinModelPortaliQ86A17.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
InParanoidiQ86A17.
KOiK00357.
OMAiNRKSMPD.
PhylomeDBiQ86A17.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86A17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKNILVLGG SGALGAEVVK FFKSKSWNTI SIDFRENPNA DHSFTIKDSG
60 70 80 90 100
EEEIKSVIEK INSKSIKVDT FVCAAGGWSG GNASSDEFLK SVKGMIDMNL
110 120 130 140 150
YSAFASAHIG AKLLNQGGLF VLTGASAALN RTSGMIAYGA TKAATHHIIK
160 170 180 190 200
DLASENGGLP AGSTSLGILP VTLDTPTNRK YMSDANFDDW TPLSEVAEKL
210 220 230
FEWSTNSDSR PTNGSLVKFE TKSKVTTWTN L
Length:231
Mass (Da):24,651
Last modified:June 1, 2003 - v1
Checksum:i0D5E03DFF4F6AA14
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000008 Genomic DNA. Translation: EAL70979.1.
RefSeqiXP_644903.1. XM_639811.1.

Genome annotation databases

EnsemblProtistsiDDB0237752; DDB0237752; DDB_G0272684.
GeneIDi8618582.
KEGGiddi:DDB_G0272684.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000008 Genomic DNA. Translation: EAL70979.1.
RefSeqiXP_644903.1. XM_639811.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ORFX-ray2.16A/B/C/D1-231[»]
ProteinModelPortaliQ86A17.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-8198634.
STRINGi44689.DDB0237752.

Proteomic databases

PaxDbiQ86A17.
PRIDEiQ86A17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0237752; DDB0237752; DDB_G0272684.
GeneIDi8618582.
KEGGiddi:DDB_G0272684.

Organism-specific databases

dictyBaseiDDB_G0272684. qdpr.

Phylogenomic databases

eggNOGiKOG4022. Eukaryota.
ENOG4111D6J. LUCA.
InParanoidiQ86A17.
KOiK00357.
OMAiNRKSMPD.
PhylomeDBiQ86A17.

Enzyme and pathway databases

BRENDAi1.5.1.34. 1939.
ReactomeiR-DDI-71182. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

PROiQ86A17.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  3. "Crystallization and preliminary characterization of dihydropteridine reductase from Dictyostelium discoideum."
    Chen C., Seo K.H., Kim H.L., Zhuang N., Park Y.S., Lee K.H.
    Acta Crystallogr. F 64:1013-1015(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, CRYSTALLIZATION.

Entry informationi

Entry nameiDHPR_DICDI
AccessioniPrimary (citable) accession number: Q86A17
Secondary accession number(s): Q559B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2003
Last modified: April 13, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.