Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7VD18 (Q7VD18_PROMA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 54. Feed History...

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

Names and origin

Protein namesRecommended name:
Dihydroorotase HAMAP MF_00219
Short name=DHOase HAMAP MF_00219
EC=3.5.2.3 HAMAP MF_00219
Gene names
Name:pyrC HAMAP MF_00219 EMBL AAP99616.1
Ordered Locus Names:Pro_0571
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219 RuleBase RU003440 SAAS SAAS004721

Subunit structure

Homodimer By similarity. HAMAP MF_00219 SAAS SAAS004721

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily. HAMAP MF_00219 RuleBase RU003440

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding151Zinc 1 By similarity HAMAP MF_00219
Metal binding171Zinc 1 By similarity HAMAP MF_00219
Metal binding1011Zinc 1; via carbamate group By similarity HAMAP MF_00219
Metal binding1011Zinc 2; via carbamate group By similarity HAMAP MF_00219
Metal binding1381Zinc 2 By similarity HAMAP MF_00219
Metal binding1761Zinc 2 By similarity HAMAP MF_00219
Metal binding2491Zinc 1 By similarity HAMAP MF_00219

Amino acid modifications

Modified residue1011N6-carboxylysine By similarity HAMAP MF_00219

Sequences

Sequence LengthMass (Da)Tools
Q7VD18 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: AF14E2A59F93DEC1

FASTA35940,260
        10         20         30         40         50         60 
MSKERITLRQ PDDWHLHLRD GDILNAVVPP TAKVFRRAVV MPNLQPPITS LQAAIDYKQR 

        70         80         90        100        110        120 
IMNAIPTEVA FTPLMTVYLT DDISSEVLRE GHKEGVLMAA KLYPANSTTN SSGGVTDIKN 

       130        140        150        160        170        180 
IYSIFETMEE IGLPLLIHGE VTDQDVDIFD RESVFIERYL DPLLTKFPDI RTVLEHITTD 

       190        200        210        220        230        240 
DAVQYVQASN AKLAATITPH HLHINRNAIF QDGLRSDFFC LPVAKRERHR IALRRAAISG 

       250        260        270        280        290        300 
EPCFFLGTDS APHLRESKES ACGCAGIFNA INAIESYAQV FDEEGAIERL EAFASEFGPA 

       310        320        330        340        350 
FYKLPLNENS ITLVKKAIKI PSRFELNNAD DLSNYIVPFH AGETLNWSFE SIQPFSQKV

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed: 12917486] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017126 Genomic DNA. Translation: AAP99616.1.
RefSeqNP_874964.1. NC_005042.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
ProteinModelPortalQ7VD18.
SMRQ7VD18. Positions 4-350.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1461953.
GenomeReviewsGene locus Pro_0571 in contig AE017126_GR.
KEGGpma:Pro0571.
PATRIC23027775. VBIProMar8617_0586.

Phylogenomic databases

HOGENOMHBG628648.
OMACLPVAKR.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycPMAR167539:PRO_0571-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. PyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ7VD18_PROMA
AccessionPrimary (citable) accession number: Q7VD18
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: December 14, 2011
This is version 54 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