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Q74J32 (PYRC_LACJO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:LJ_1278
OrganismLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]
Taxonomic identifier257314 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B

Subunit structure

Homodimer By similarity. HAMAP MF_00220_B

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: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Dihydroorotase HAMAP MF_00220_B
PRO_1000024090

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

Sequences

Sequence LengthMass (Da)Tools
Q74J32 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 99C2F52414311027

FASTA42546,053
        10         20         30         40         50         60 
MTTVIKNGTV YQNGHLIKAD VLIDGQKIKA IGTDLEGEEI IDASGMIVSP GLVDVHVHYR 

        70         80         90        100        110        120 
DPGQTYKEDI KTGSQAAARG GFTTVGAMPN VTPVPNTAEL MDKMVRENQK KGLVHILQYG 

       130        140        150        160        170        180 
PVTNDETTDI IPDYAALKKA GAFALSNDGH GVQSAQTMYL AMQKAKENNL IIAAHAQDDS 

       190        200        210        220        230        240 
LFNKGIVNEG IAAEKLDLPP VTELAETTQI ARDLLLAQKT GVHYHICHVS TKTSVELVRL 

       250        260        270        280        290        300 
AKARGIKVTC EVAPHHILLT DSDIPEDNAY FKMNPPLRSK EDQVALLVGL LDGTIDLIAT 

       310        320        330        340        350        360 
DHAPHAKAEK QGGMRGAAFG ITGSETAFST LYTRFVKEEK VFTLEQLLSL LTDKPATVFG 

       370        380        390        400        410        420 
IENAGLLAPG ENADIAIFDI EHQREIKEDD FKSKGVNTPF TGHKVYGETV MTFVDGKVVY 


QRGTK

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References

[1]"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533."
Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.
Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed: 14983040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017198 Genomic DNA. Translation: AAS09099.1.
RefSeqNP_965133.1. NC_005362.1.

3D structure databases

HSSPHSSP built from PDB template 1XRT based on UniProtKB O66990.
ProteinModelPortalQ74J32.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2743536.
GenomeReviewsGene locus LJ_1278 in contig AE017198_GR.
KEGGljo:LJ1278.
NMPDRfig|257314.1.peg.1119.
PATRIC22238937. VBILacJoh1832_1146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG724623.
OMANRWLLFD.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycLJOH257314:LJ_1278-MONOMER.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. PyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_LACJO
AccessionPrimary (citable) accession number: Q74J32
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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