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Protein
Submitted name:

DHODH protein

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201FMNCombined sources
Binding sitei68 – 681FMNCombined sources
Binding sitei128 – 1281FMNCombined sources
Active sitei131 – 1311NucleophileUniRule annotation
Binding sitei165 – 1651FMNCombined sources
Binding sitei223 – 2231FMN; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 452FMNCombined sources
Nucleotide bindingi194 – 1952FMNCombined sources
Nucleotide bindingi249 – 2513FMNCombined sources
Nucleotide bindingi272 – 2732FMNCombined sources

GO - Molecular functioni

  1. dihydroorotate dehydrogenase activity Source: GeneDB
  2. dihydroorotate oxidase activity Source: UniProtKB-EC
  3. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: GeneDB
  2. fumarate metabolic process Source: GeneDB
  3. 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:
DHODH proteinImported (EC:1.3.3.1Imported)
Gene namesi
Name:DHODHImported
ORF Names:LMJF_16_0530Imported
OrganismiLeishmania majorImported
Taxonomic identifieri5664 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania
ProteomesiUP000000542 Componenti: Chromosome 16

Subcellular locationi

GO - Cellular componenti

  1. glycosome Source: GeneDB
Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ4QEW7.

Family & Domainsi

Phylogenomic databases

HOGENOMiHOG000225104.
InParanoidiQ4QEW7.
KOiK00226.
OMAiVSCPHAE.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
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.
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
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. Positions 1-313.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000225104.
InParanoidiQ4QEW7.
KOiK00226.
OMAiVSCPHAE.

Miscellaneous databases

EvolutionaryTraceiQ4QEW7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the kinetoplastid parasite, Leishmania major."
    Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G., Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A., Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M., Bianchettin G.
    , Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E., Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M., De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N., Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A., Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S., Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M., Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S., Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M., Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E., Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C., Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K., Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V., Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J., Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D., Barrell B., Myler P.J.
    Science 309:436-442(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MHOM/IL/81/FriedlinImported.
  2. "Crystal Structure of Leishmania major Dihydroorotate dehydrogenase."
    Cordeiro A.T., Feliciano P.R., Nonato M.C.
    Submitted (APR-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH FMN.
  3. "Leismania major dihydroorotate in complex with orotate."
    Cordeiro A.T., Feliciano P.R., Nonato M.C.
    Submitted (APR-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FMN.
  4. "Novel insights for dihydroorotate dehydrogenase class 1A inhibitors discovery."
    Cheleski J., Rocha J.R., Pinheiro M.P., Wiggers H.J., da Silva A.B., Nonato M.C., Montanari C.A.
    Eur. J. Med. Chem. 45:5899-5909(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-312 IN COMPLEX WITH FMN.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FriedlinImported.
  6. "Crystal Structure of Leishmania major dihydroorotate dehydrogenase mutant H174A."
    de Souza A.L., Nonato M.C., Pinheiro M.P.
    Submitted (AUG-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH FMN.
  7. "Crystal Structure of Leishmania major dihydroorotate dehydrogenase mutant D171A."
    de Souza A.L., Pinheiro M.P., Nonato M.C.
    Submitted (SEP-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH FMN.
  8. "Crystal structure of dihydroorotate dehydrogenase from Leishmania major."
    Cordeiro A.T., Feliciano P.R., Pinheiro M.P., Nonato M.C.
    Biochimie 94:1739-1748(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-312 IN COMPLEX WITH FMN.
  9. "Target sites for the design of anti-trypanosomatid drugs based on the structure of dihydroorotate dehydrogenase."
    Pinheiro M.P., Emery F.d.a. .S., Nonato M.C.
    Curr. Pharm. Des. 19:2615-2627(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH FMN.

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: April 29, 2015
This is version 83 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

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.