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Reviewed, UniProtKB/Swiss-Prot Q5FJB8 (PYRC_LACAC)

Last modified September 2, 2008. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: LBA1381
OrganismLactobacillus acidophilus [Complete proteome] [HAMAP]
Taxonomic identifier1579 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

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Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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Ontologies

Keywords

   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Dihydroorotase
PRO_1000024086

Sites

Metal binding561Zinc 1 By similarity
Metal binding581Zinc 1 By similarity
Metal binding1381Zinc 1; via carbamate group By similarity
Metal binding1381Zinc 2; via carbamate group By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2281Zinc 2 By similarity
Metal binding3011Zinc 1 By similarity

Amino acid modifications

Modified residue1381N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5FJB8-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: B620B6A643E949B6

FASTA42546,392
        10         20         30         40         50         60 
MKTVIKNGTV YQNGRLIHAD VLIEDQKIKV IGTNLTGDKE FDATGKLVAP GLVDVHVHYR 

        70         80         90        100        110        120 
EPGQTYKEDI RTGSEAAARG GFTTVGAMPN VTPVPNTPEL MEKMVKKNQE KGIVHIFQYG 

       130        140        150        160        170        180 
PITNDETTDI IPDYAALKKA GAFALSNDGH GVQTAQTMYL AMQKAKANNL IIATHAQDDS 

       190        200        210        220        230        240 
LFNHGIVNEG KKAEELNLPP VTELAETTQI ARDLLLAQKT GVHYHICHVS TKTSVELVRM 

       250        260        270        280        290        300 
AKARGINVTC EVAPHHILLT DDDIPKDNGY YKMNPPLRNK EDQAALLVGL LDGTIDLIAT 

       310        320        330        340        350        360 
DHAPHAKKEK QGGMKGAAFG ITGSETAFST LYTKFVKKDK VFTLEQLLSW LSDKPAEAFG 

       370        380        390        400        410        420 
LKDAGVLEPG KNADIAIFDI EHEATIEEKD YKSKGVNTPF TGQKVYGETV MTMVNGKVVY 


QRGTK

« Hide

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References

[1]"Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM."
Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S., Hamrick A., Cano R., Klaenhammer T.R.
Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005) [PubMed: 15671160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCFM.

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Cross-references

Sequence databases

CP000033 Genomic DNA. Translation: AAV43206.1.
RefSeqYP_194237.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Genome annotation databases

GeneID3252590.
GenomeReviewsGene locus LBA1381 in contig CP000033_GR.
KEGGlac:LBA1381.
NMPDRfig|272621.3.peg.1298.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5FJB8.

Enzyme and pathway databases

BioCycLACI272621:LBA1381-MON.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePYRC_LACAC
AccessionPrimary (citable) accession number: Q5FJB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2005
Last modified: September 2, 2008
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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