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Protein
Submitted name:

Dihydroorotate dehydrogenase

Gene

DHODH

Organism
Leishmania major
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei20FMNCombined sources1
Binding sitei44OrotateCombined sources1
Binding sitei68FMNCombined sources1
Binding sitei128FMNCombined sources1
Binding sitei128OrotateCombined sources1
Binding sitei165FMNCombined sources1
Binding sitei223FMN; via amide nitrogenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 45FMNCombined sources2
Nucleotide bindingi194 – 195FMNCombined sources2
Nucleotide bindingi249 – 251FMNCombined sources3
Nucleotide bindingi272 – 273FMNCombined sources2

GO - Molecular functioni

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: GeneDB
  • fumarate metabolic process Source: GeneDB
  • UMP biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseImported

Keywords - Ligandi

Flavoprotein, FMNCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Dihydroorotate dehydrogenaseImported (EC:1.3.3.1Imported)
Gene namesi
Name:DHODHImported
ORF Names:LMJF_16_0530Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
Proteomesi
  • UP000000542 Componenti: Chromosome 16

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Protein-protein interaction databases

STRINGi5664.LmjF.16.0530.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GYEX-ray2.00A/B1-320[»]
3GZ3X-ray1.90A/B1-320[»]
3MHUX-ray1.85A/B1-312[»]
3MJYX-ray1.96A/B1-312[»]
3TJXX-ray1.64A/B1-320[»]
3TQ0X-ray1.90A/B1-312[»]
3TROX-ray1.86A/B1-320[»]
4EF8X-ray1.56A/B1-320[»]
4EF9X-ray1.60A/B1-320[»]
ProteinModelPortaliQ4QEW7.
SMRiQ4QEW7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4QEW7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 293DHO_dhInterPro annotationAdd BLAST291

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni68 – 72Orotate bindingCombined sources5
Regioni195 – 196Orotate bindingCombined sources2

Phylogenomic databases

eggNOGiKOG1436. Eukaryota.
COG0167. LUCA.
HOGENOMiHOG000225104.
InParanoidiQ4QEW7.
KOiK00226.
OMAiVSCPHAE.

Family and domain databases

CDDicd04741. DHOD_1A_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR033886. DHOD_1A.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.

Sequencei

Sequence statusi: Complete.

Q4QEW7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLQVNLLNN TFANPFMNAA GVMCTTTEEL VAMTESASGS LVSKSCTPAL
60 70 80 90 100
REGNPTPRYQ ALPLGSINSM GLPNNGFDFY LAYAAEQHDY GKKPLFLSMS
110 120 130 140 150
GLSMRENVEM CKRLAAVATE KGVILELNLS CPNVPGKPQV AYDFDAMRQC
160 170 180 190 200
LTAVSEVYPH SFGVKMPPYF DFAHFDAAAE ILNEFPKVQF ITCINSIGNG
210 220 230 240 250
LVIDAETESV VIKPKQGFGG LGGRYVLPTA LANINAFYRR CPGKLIFGCG
260 270 280 290 300
GVYTGEDAFL HVLAGASMVQ VGTALQEEGP SIFERLTSEL LGVMAKKRYQ
310 320
TLDEFRGKVR TLDGTAESTR
Length:320
Mass (Da):34,662
Last modified:July 19, 2005 - v1
Checksum:iFB13D0101F91577A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796412 Genomic DNA. Translation: CAJ03555.1.
RefSeqiXP_001682131.1. XM_001682079.1.

Genome annotation databases

EnsemblProtistsiLmjF.16.0530:mRNA; LmjF.16.0530:pep; LmjF.16.0530.
GeneDBiLmjF.16.0530:pep.
GeneIDi5650598.
KEGGilma:LMJF_16_0530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FR796412 Genomic DNA. Translation: CAJ03555.1.
RefSeqiXP_001682131.1. XM_001682079.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GYEX-ray2.00A/B1-320[»]
3GZ3X-ray1.90A/B1-320[»]
3MHUX-ray1.85A/B1-312[»]
3MJYX-ray1.96A/B1-312[»]
3TJXX-ray1.64A/B1-320[»]
3TQ0X-ray1.90A/B1-312[»]
3TROX-ray1.86A/B1-320[»]
4EF8X-ray1.56A/B1-320[»]
4EF9X-ray1.60A/B1-320[»]
ProteinModelPortaliQ4QEW7.
SMRiQ4QEW7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5664.LmjF.16.0530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiLmjF.16.0530:mRNA; LmjF.16.0530:pep; LmjF.16.0530.
GeneDBiLmjF.16.0530:pep.
GeneIDi5650598.
KEGGilma:LMJF_16_0530.

Phylogenomic databases

eggNOGiKOG1436. Eukaryota.
COG0167. LUCA.
HOGENOMiHOG000225104.
InParanoidiQ4QEW7.
KOiK00226.
OMAiVSCPHAE.

Miscellaneous databases

EvolutionaryTraceiQ4QEW7.

Family and domain databases

CDDicd04741. DHOD_1A_like. 1 hit.
Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR033886. DHOD_1A.
IPR005720. Dihydroorotate_DH.
IPR012135. Dihydroorotate_DH_1_2.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiQ4QEW7_LEIMA
AccessioniPrimary (citable) accession number: Q4QEW7
Entry historyi
Integrated into UniProtKB/TrEMBL: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 30, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.