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Reviewed, UniProtKB/Swiss-Prot Q38X26 (PYRC_LACSS)

Last modified September 2, 2008. Version 25. 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

Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: LSA0953
OrganismLactobacillus sakei subsp. sakei (strain 23K) [Complete proteome] [HAMAP]
Taxonomic identifier314315 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 429429Dihydroorotase
PRO_1000024092

Sites

Metal binding621Zinc 1 By similarity
Metal binding641Zinc 1 By similarity
Metal binding1441Zinc 1; via carbamate group By similarity
Metal binding1441Zinc 2; via carbamate group By similarity
Metal binding1811Zinc 2 By similarity
Metal binding2341Zinc 2 By similarity
Metal binding3071Zinc 1 By similarity

Amino acid modifications

Modified residue1441N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q38X26-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 7F40A19F45F0FEEB

FASTA42945,772
        10         20         30         40         50         60 
MYRLIQNGQL LIDDQLVKRD IAIDEKGRIT AIEAQITPTD EPTETIFDAQ GALVSAGLID 

        70         80         90        100        110        120 
GHVHFRDPGF TDKETLQTGS QAAAHGGYTS VIAMPNLNPV PDNLSDFKTL VARNQTETSV 

       130        140        150        160        170        180 
HTYQFAPITG DLVNNDLVDM PAFKAAGAAG FTNDGHGVQD AQTMYLAMQQ AAAIDAPIVA 

       190        200        210        220        230        240 
HVEDISLVNG GVIHDGAAAK RLNVPGIPSV SESAQVARDI ELARATGVHY HICHISTKET 

       250        260        270        280        290        300 
VALVRRAKAD GVNITCEVTP HHLLLDDRSI ISDDTMLKMN PPLRTLADRQ SLWAGLMDGT 

       310        320        330        340        350        360 
IDVIATDHAP HTAAEKSQSL LQAPFGIVGS ETAFSLLYTH LVVNGPFSLA QLLAKMTTVP 

       370        380        390        400        410        420 
AQVFNLPAAG QLRVGDQADI AVFNLTQPTT IQATDFQSKG HNTPFIGETV LGGTELTLVA 


GQVAYQRSK 

« Hide

References

[1]"The complete genome sequence of the meat-borne lactic acid bacterium Lactobacillus sakei 23K."
Chaillou S., Champomier-Verges M.-C., Cornet M., Crutz-Le Coq A.-M., Dudez A.-M., Martin V., Beaufils S., Darbon-Rongere E., Bossy R., Loux V., Zagorec M.
Nat. Biotechnol. 23:1527-1533(2005) [PubMed: 16273110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR936503 Genomic DNA. Translation: CAI55255.1.
RefSeqYP_395564.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3777487.
GenomeReviewsGene locus LSA0953 in contig CR936503_GR.
KEGGlsa:LSA0953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ38X26.

Enzyme and pathway databases

BioCycLSAK314315:LSA0953-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...

Entry information

Entry namePYRC_LACSS
AccessionPrimary (citable) accession number: Q38X26
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: September 2, 2008
This is version 25 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)

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