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Protein

Dihydroorotate dehydrogenase (quinone), mitochondrial

Gene

SELMODRAFT_440247

Organism
Selaginella moellendorffii (Spikemoss)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

FMNUniRule annotationNote: Binds 1 FMN per subunit.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. dihydroorotate dehydrogenase activity Source: UniProtKB-EC

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  2. UMP biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Ligandi

Flavoprotein, FMNUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone), mitochondrialUniRule annotation (EC:1.3.5.2UniRule annotation)
Short name:
DHOdehaseUniRule annotation
Gene namesi
ORF Names:SELMODRAFT_440247Imported
OrganismiSelaginella moellendorffii (Spikemoss)Imported
Taxonomic identifieri88036 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaLycopodiidaeSelaginellalesSelaginellaceaeSelaginella
ProteomesiUP000001514: Unassembled WGS sequence

Subcellular locationi

Mitochondrion inner membrane UniRule annotation; Single-pass membrane protein UniRule annotation

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membraneUniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

InParanoidiD8RAG3.
KOiK00254.
OMAiIPQEGNP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D8RAG3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MREGRLLAAI ARRFAYGSSS CIHTAAETSG SAKEAVAAAF QKPPLPPKIR
60 70 80 90 100
LTWGRVLTGT LLGAVIAGGA YVGTRDEATI SAWTFEAAKY INPLFRLLDP
110 120 130 140 150
ENAHKVAIWA SSHCLCPRET RPDPPVLEVS VWGRTFSNPV GLAAGFDKNA
160 170 180 190 200
EAVEGLLGIG FGFMEVGSVT PVPQEGNPKP RVFRLPEQGA IINRYGFNSE
210 220 230 240 250
GIVAVAKRLG AQHGKRRMAE TVNSAITTNT EQRVLGGKAG PGILGVNLGK
260 270 280 290 300
NKTSEDAAAD YVQGVHTLSQ YADYLVINVS SPNTPGLRKL QGRKQLKDLI
310 320 330 340 350
KKVLAARDEM QWGEEGPPPL LVKIAPDLSK QDLADIAAVA LSLRLDGLII
360 370 380 390 400
ANTTVSRPDS VIGLVHADEM GGLSGKPLFT LSTEVLREMY QLTWGKIPLV
410 420 430 440 450
GCGGISSGEE AYVKIRAGAT LVQLYTTFAY EGPALIPRIK AELAACLERD
460
GFKSAQEAIG ADHR
Length:464
Mass (Da):49,511
Last modified:October 5, 2010 - v1
Checksum:iE1574FF94CF98AF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377575 Genomic DNA. Translation: EFJ30613.1.
RefSeqiXP_002968359.1. XM_002968313.1.
UniGeneiSmo.7808.

Genome annotation databases

EnsemblPlantsiEFJ30613; EFJ30613; SELMODRAFT_440247.
GeneIDi9631151.
KEGGismo:SELMODRAFT_440247.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GL377575 Genomic DNA. Translation: EFJ30613.1.
RefSeqiXP_002968359.1. XM_002968313.1.
UniGeneiSmo.7808.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEFJ30613; EFJ30613; SELMODRAFT_440247.
GeneIDi9631151.
KEGGismo:SELMODRAFT_440247.

Phylogenomic databases

InParanoidiD8RAG3.
KOiK00254.
OMAiIPQEGNP.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00946.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamiPF01180. DHO_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The Selaginella genome identifies genetic changes associated with the evolution of vascular plants."
    Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M., dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W., Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D., Chapple C., Cheng C.
    , Correa L.G., Dacre M., DeBarry J., Dreyer I., Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K., Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M., Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G., Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y., Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K., Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R., Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B., Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y., Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N., Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N., Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S., Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q., Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J., Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.
    Science 332:960-963(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiD8RAG3_SELML
AccessioniPrimary (citable) accession number: D8RAG3
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: March 4, 2015
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

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.