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A3PBU3 (A3PBU3_PROM0) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 41. 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 names
EC=3.5.2.3 EMBL ABO17218.1
Gene names
Ordered Locus Names:P9301_05951
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP] EMBL ABO17218.1
Taxonomic identifier167546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. SAAS SAAS004721

Cofactor

Binds 2 zinc ions per subunit By similarity. SAAS SAAS004721

Pathway

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

Subunit structure

Homodimer By similarity. SAAS SAAS004721

Sequences

Sequence LengthMass (Da)Tools
A3PBU3 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 1816077F7079A8CF

FASTA34939,638
        10         20         30         40         50         60 
MKTLTIIKPD DWHLHLREGL VLKNIIHFTS EYFGRAIVMP NTKVPITSIK SAISYKKSII 

        70         80         90        100        110        120 
EALPESSKFK PLMTMYLTDE TDKGELINGF KNNVFFAAKL YPANATTNSS HGVRKIENLY 

       130        140        150        160        170        180 
KIFESMQDSG MPLLIHGEVT DSEVDVFDRE EVFIDKELSQ ITKRFPKLKI VLEHITTSYA 

       190        200        210        220        230        240 
VNFVKENNIG ATITPHHLHI NRNAMFFGGL NSDFYCLPVA KRENNRLALR KAATSGEKCF 

       250        260        270        280        290        300 
FLGTDSAPHL RKWKAFCGCA GIFNSPVAIE SYLTVFEEED ALDNFEKFAS LNGPNFYNVP 

       310        320        330        340 
PNKEKLKLVS RPNKIKEFID VIQEKNTVGQ IKPFHAGETL QWQVEGKLI 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO17218.1.
RefSeqYP_001090819.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PBU3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3PBU3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4911368.
GenomeReviewsGene locus P9301_05951 in contig CP000576_GR.
KEGGpmg:P9301_05951.
PATRIC22994783. VBIProMar103344_0581.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHBG628648.
OMACLPVAKR.
PhylomeDBA3PBU3.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycPMAR167546:P9301ORF_0609-MONOMER.

Family and domain databases

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 nameA3PBU3_PROM0
AccessionPrimary (citable) accession number: A3PBU3
Entry history
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)