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A7ZYP7

- PYRD_ECOHS

UniProt

A7ZYP7 - PYRD_ECOHS

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Protein
Dihydroorotate dehydrogenase (quinone)
Gene
pyrD, EcHS_A1054
Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Binds 1 FMN per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei66 – 661Substrate By similarity
Binding sitei86 – 861FMN; via amide nitrogen By similarity
Binding sitei139 – 1391FMN By similarity
Binding sitei172 – 1721FMN By similarity
Binding sitei172 – 1721Substrate By similarity
Active sitei175 – 1751Nucleophile By similarity
Binding sitei177 – 1771Substrate By similarity
Binding sitei217 – 2171FMN By similarity
Binding sitei245 – 2451FMN; via carbonyl oxygen By similarity
Binding sitei268 – 2681FMN; via amide nitrogen By similarity
Binding sitei297 – 2971FMN; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi62 – 665FMN By similarity
Nucleotide bindingi318 – 3192FMN By similarity

GO - Molecular functioni

  1. dihydroorotate oxidase activity Source: InterPro

GO - Biological processi

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

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN

Enzyme and pathway databases

BioCyciECOL331112:GHHI-1048-MONOMER.
UniPathwayiUPA00070; UER00946.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydroorotate dehydrogenase (quinone) (EC:1.3.5.2)
Alternative name(s):
DHOdehase
Short name:
DHOD
Short name:
DHODase
Dihydroorotate oxidase
Gene namesi
Name:pyrD
Ordered Locus Names:EcHS_A1054
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001123: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Dihydroorotate dehydrogenase (quinone)UniRule annotation
PRO_1000058682Add
BLAST

Proteomic databases

PRIDEiA7ZYP7.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi331112.EcHS_A1054.

Structurei

3D structure databases

ProteinModelPortaliA7ZYP7.
SMRiA7ZYP7. Positions 1-336.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1155Substrate binding By similarity
Regioni246 – 2472Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0167.
HOGENOMiHOG000225103.
KOiK00254.
OMAiGECIDAF.
OrthoDBiEOG65BDN8.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00225. DHO_dh_type2.
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]
PIRSFiPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsiTIGR01036. pyrD_sub2. 1 hit.
PROSITEiPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A7ZYP7-1 [UniParc]FASTAAdd to Basket

« Hide

MYYPFVRKAL FQLDPERAHE FTFQQLRRIT GTPFEALVRQ KVPAKPVNCM    50
GLTFKNPLGL AAGLDKDGEC IDALGAMGFG SIEIGTVTPR PQPGNDKPRL 100
FRLVDAEGLI NRMGFNNLGV DNLVENVKKA HYDGVLGINI GKNKDTPVEQ 150
GKDDYLICME KIYAYAGYIA INISSPNTPG LRTLQYGEAL DDLLTAIKNK 200
QNDLQAMHHK YVPIAVKIAP DLSEEELIQV ADSLVRHNID GVIATNTTLD 250
RSLVQGMKNC DQTGGLSGRP LQLKSTEIIR RLSLELNGRL PIIGVGGIDS 300
VIAAREKIAA GASLVQIYSG FIFKGPPLIK EIVTHI 336
Length:336
Mass (Da):36,775
Last modified:October 23, 2007 - v1
Checksum:i973227EAE6B83622
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV05401.1.
RefSeqiYP_001457784.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV05401; ABV05401; EcHS_A1054.
GeneIDi5592134.
KEGGiecx:EcHS_A1054.
PATRICi18312092. VBIEscCol77814_1023.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000802 Genomic DNA. Translation: ABV05401.1 .
RefSeqi YP_001457784.1. NC_009800.1.

3D structure databases

ProteinModelPortali A7ZYP7.
SMRi A7ZYP7. Positions 1-336.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 331112.EcHS_A1054.

Proteomic databases

PRIDEi A7ZYP7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV05401 ; ABV05401 ; EcHS_A1054 .
GeneIDi 5592134.
KEGGi ecx:EcHS_A1054.
PATRICi 18312092. VBIEscCol77814_1023.

Phylogenomic databases

eggNOGi COG0167.
HOGENOMi HOG000225103.
KOi K00254.
OMAi GECIDAF.
OrthoDBi EOG65BDN8.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00946 .
BioCyci ECOL331112:GHHI-1048-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00225. DHO_dh_type2.
InterProi IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view ]
Pfami PF01180. DHO_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsi TIGR01036. pyrD_sub2. 1 hit.
PROSITEi PS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiPYRD_ECOHS
AccessioniPrimary (citable) accession number: A7ZYP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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