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P32748 (PYRD_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrial
Short name=DHOdehase
Short name=Dihydroorotate oxidase
EC=1.3.5.2
Gene names
Name:Dhod
ORF Names:CG9741
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity.

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol.

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1.

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein Potential.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Sequence caution

The sequence AAB59185.1 differs from that shown. Reason: Frameshift at positions 378 and 391.

The sequence AAQ22565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAA35184.1 differs from that shown. Reason: Frameshift at positions 365, 374 and 394.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 405Dihydroorotate dehydrogenase (quinone), mitochondrialPRO_0000029887

Regions

Topological domain? – 20Mitochondrial matrix Potential
Transmembrane21 – 3919Helical; Potential
Topological domain40 – 401362Mitochondrial intermembrane Potential
Nucleotide binding103 – 1075FMN By similarity
Nucleotide binding361 – 3622FMN By similarity
Region152 – 1565Substrate binding By similarity
Region215 – 2206Substrate binding By similarity
Region289 – 2902Substrate binding By similarity

Sites

Active site2181Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1271FMN By similarity
Binding site1841FMN By similarity
Binding site2151FMN By similarity
Binding site2151Substrate By similarity
Binding site2581FMN By similarity
Binding site2881FMN; via carbonyl oxygen By similarity
Binding site3111FMN; via amide nitrogen By similarity
Binding site3401FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P32748 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 875F32BBED8BCC9D

FASTA40544,342
        10         20         30         40         50         60 
MDQDHLKNAK NATRRVGRLR SLGIVTVGGA ALVAGITAYK NQDQLFRTFV MPAVRLLPAE 

        70         80         90        100        110        120 
ASHQLAVLAC KYRLCPVSQY HDDQNLHTSF FGRMLSNPIG IAAGFDKNAE AVDGLQDLGF 

       130        140        150        160        170        180 
GFIEVGTVTP AAQEGNPKPR VFRLTEDKAI INRYGFNSDG HQAVLQRLRL LRKKENFNGV 

       190        200        210        220        230        240 
VGVNLGRNKT TMSPIADYVQ GVRVFGPVAD YLVINVSSPN TKGLRDMQSK EKLRELLEQV 

       250        260        270        280        290        300 
NDTKSSLDKN KNVPILLKLS PDLSLDDMKD IVWVIKRKKS RVDGLIVSNT TVSRENIEKN 

       310        320        330        340        350        360 
KLAEETGGLS GPPLKARSTE MIAQMYQLTD GKIPIIGVGG VASGYDAYEK IEAGASYVQI 

       370        380        390        400 
YTALVYEGPA LVEDIKAELS ALITRLGHTN VADVVGTNSK FYLPK

« Hide

References

« Hide 'large scale' references
[1]"The dhod gene and deduced structure of mitochondrial dihydroorotate dehydrogenase in Drosophila melanogaster."
Rawls J., Kirkpatrick R., Yang J., Lacy L.
Gene 124:191-197(1993) [PubMed: 8444342] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo and Head.
[5]"Molecular cloning and transcript mapping of the dihydroorotate dehydrogenase dhod locus of Drosophila melanogaster."
Jones W.K., Kirkpatrick R., Rawls J.M.
Mol. Gen. Genet. 219:397-403(1989) [PubMed: 2482933] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 325-405.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L00964 Genomic DNA. Translation: AAB59185.1. Frameshift.
AE014297 Genomic DNA. Translation: AAF54260.1.
AE014297 Genomic DNA. Translation: AAN13391.2.
BT009968 mRNA. Translation: AAQ22437.1.
BT010096 mRNA. Translation: AAQ22565.1. Different initiation.
X17297 mRNA. Translation: CAA35184.1. Frameshift.
PIRJN0500.
S15742.
RefSeqNP_477224.1. NM_057876.4.
NP_599138.3. NM_134311.3.
UniGeneDm.7901.

3D structure databases

ProteinModelPortalP32748.
SMRP32748. Positions 39-401.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-23907N.
IntActP32748. 1 interaction.
MINTMINT-742593.
STRINGP32748.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081890; FBpp0081376; FBgn0000447.
FBtr0300442; FBpp0289671; FBgn0000447.
GeneID41022.
KEGGdme:Dmel_CG9741.

Organism-specific databases

CTD41022.
FlyBaseFBgn0000447. Dhod.

Phylogenomic databases

eggNOGinNOG06457.
GeneTreeEMGT00050000010553.
InParanoidP32748.
OMAAALNRMG.
OrthoDBEOG43BK4M.
PhylomeDBP32748.

Gene expression databases

BgeeP32748.
GermOnlineCG9741. Drosophila melanogaster.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00254.
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio821763.

Entry information

Entry namePYRD_DROME
AccessionPrimary (citable) accession number: P32748
Secondary accession number(s): Q8INQ4, Q8INQ5, Q9VHP2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents