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E1U9B3 (E1U9B3_LISML) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotase HAMAP-Rule MF_00220
Short name=DHOase HAMAP-Rule MF_00220
EC=3.5.2.3 HAMAP-Rule MF_00220
Gene names
Name:pyrC HAMAP-Rule MF_00220 EMBL CAR84598.1
Ordered Locus Names:lmo4a_1894 EMBL CAR84598.1
OrganismListeria monocytogenes serotype 4a (strain L99) [Complete proteome] [HAMAP]
Taxonomic identifier563174 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria ›

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00220 SAAS SAAS002195

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00220 SAAS SAAS004722

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule MF_00220 SAAS SAAS002195

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00220 SAAS SAAS002195

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily. HAMAP-Rule MF_00220

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding581Zinc 1 By similarity HAMAP-Rule MF_00220
Metal binding601Zinc 1 By similarity HAMAP-Rule MF_00220
Metal binding1401Zinc 1; via carbamate group By similarity HAMAP-Rule MF_00220
Metal binding1401Zinc 2; via carbamate group By similarity HAMAP-Rule MF_00220
Metal binding1771Zinc 2 By similarity HAMAP-Rule MF_00220
Metal binding2301Zinc 2 By similarity HAMAP-Rule MF_00220
Metal binding3031Zinc 1 By similarity HAMAP-Rule MF_00220

Amino acid modifications

Modified residue1401N6-carboxylysine By similarity HAMAP-Rule MF_00220

Sequences

Sequence LengthMass (Da)Tools
E1U9B3 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: 3B40D88BB5FE7451

FASTA42646,056
        10         20         30         40         50         60 
MYVLKNGQVL NASGELENKD VLIQNGKVNL IADSIEVTSG EEFDATGKLI APGFIDVHVH 

        70         80         90        100        110        120 
LREPGGEHKE TILTGTQAAA RGGYTTICSM PNTKPVPDSK EVMENLQAKI KETAEVRVLP 

       130        140        150        160        170        180 
YASITTSLGT DELVDFEALK EAGAFAFTDD GVGVQLAGTM YEAMKRAAAL DMAIVAHCED 

       190        200        210        220        230        240 
NSLIYGGVVH DGIFAEKEGL KGIPNIAESV QIARDVLLAE AAGCHYHVCH ISTKESVRVV 

       250        260        270        280        290        300 
RDAKRAGIRV TAEVSPHHLI LDEEAIPGND GNWKMNPPLR SKADRAALLE GLLDGTIDFI 

       310        320        330        340        350        360 
ATDHAPHAAE EKNVPMEQAA FGIVGLETGF PLLYTHFVKT NEWTLKQLID WMTVKPAECF 

       370        380        390        400        410        420 
KLPYGKLEEG SVADIVVLDL EKEATIDPAT FYSKGKNTPF VGETCIGWPV ATFAEGTLVY 


NEGEIK

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References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM211688 Genomic DNA. Translation: CAR84598.1.
RefSeqYP_005926887.1. NC_017529.1.

3D structure databases

ProteinModelPortalE1U9B3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR84598; CAR84598; lmo4a_1894.
GeneID12517172.
KEGGlml:lmo4a_1894.
PATRIC43109896. VBILisMon174077_1949.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000219142.
KOK01465.
OMAGKNSPFI.

Enzyme and pathway databases

UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameE1U9B3_LISML
AccessionPrimary (citable) accession number: E1U9B3
Entry history
Integrated into UniProtKB/TrEMBL: November 30, 2010
Last sequence update: November 30, 2010
Last modified: May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info