Dihydroorotate dehydrogenase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0A7E1 (PYRD_ECOLI)

Last modified November 3, 2009. Version 51. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.5.2
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD

Gene names

Name:	pyrD
Ordered Locus Names:	b0945, JW0928

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Hide | Top

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP MF_00225
Cofactor	Binds 1 FMN per subunit. HAMAP MF_00225
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP MF_00225
Subunit structure	Homodimer. HAMAP MF_00225
Subcellular location	Cell membrane; Peripheral membrane protein. HAMAP MF_00225
Sequence similarities	Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Hide | Top

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Cellular component	Cell membrane Membrane
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro UMP biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 336

336

Dihydroorotate dehydrogenase HAMAP MF_00225

PRO_0000148437

Sites

Active site

175

Nucleophile HAMAP MF_00225

Secondary structure

336

Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P0A7E1-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 973227EAE6B83622
Show »

FASTA

336

36,775

        10         20         30         40         50         60 
MYYPFVRKAL FQLDPERAHE FTFQQLRRIT GTPFEALVRQ KVPAKPVNCM GLTFKNPLGL 

        70         80         90        100        110        120 
AAGLDKDGEC IDALGAMGFG SIEIGTVTPR PQPGNDKPRL FRLVDAEGLI NRMGFNNLGV 

       130        140        150        160        170        180 
DNLVENVKKA HYDGVLGINI GKNKDTPVEQ GKDDYLICME KIYAYAGYIA INISSPNTPG 

       190        200        210        220        230        240 
LRTLQYGEAL DDLLTAIKNK QNDLQAMHHK YVPIAVKIAP DLSEEELIQV ADSLVRHNID 

       250        260        270        280        290        300 
GVIATNTTLD RSLVQGMKNC DQTGGLSGRP LQLKSTEIIR RLSLELNGRL PIIGVGGIDS 

       310        320        330 
VIAAREKIAA GASLVQIYSG FIFKGPPLIK EIVTHI

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the pyrD gene of Escherichia coli and characterization of the flavoprotein dihydroorotate dehydrogenase." Larsen N.J., Jensen K.F. Eur. J. Biochem. 151:59-65(1985) [PubMed: 2992959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases." Noerager S., Jensen K.F., Bjoernberg O., Larsen S. Structure 10:1211-1223(2002) [PubMed: 12220493] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Hide | Top

Cross-references

Sequence databases

X02826 Genomic DNA. Translation: CAA26594.1.
U00096 Genomic DNA. Translation: AAC74031.1.
AP009048 Genomic DNA. Translation: BAA35700.1.

PIR

DEECDO. A23109.

RefSeq

AP_001575.1.
NP_415465.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F76	X-ray	2.50	A/B/D/E	1-336	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A7E1.

2-D gel databases

SWISS-2DPAGE

P0A7E1.

Proteomic databases

PRIDE

P0A7E1.

Genome annotation databases

GeneID

945556.

GenomeReviews

Gene locus JW0928 in contig AP009048_GR.
Gene locus b0945 in contig U00096_GR.

KEGG

ecj:JW0928.
eco:b0945.

Organism-specific databases

EchoBASE

EB0800.

EcoGene

EG10807. pyrD.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A7E1.

OMA

NAEQQGG.

Enzyme and pathway databases

BioCyc

EcoCyc:DIHYDROOROTOX-MON.
MetaCyc:DIHYDROOROTOX-MON.

Gene expression databases

Genevestigator

P0A7E1.

Family and domain databases

HAMAP

MF_00225.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01180. DHO_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF000164. DHO_oxidase. 1 hit.

TIGRFAMs

TIGR01036. pyrD_sub2. 1 hit.

PROSITE

PS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Hide | Top

Entry information

Entry name

PYRD_ECOLI

Accession

Primary (citable) accession number: P0A7E1
Secondary accession number(s): P05021

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	November 3, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top