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Q1AVY7 (PYRC_RUBXD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:Rxyl_1479
OrganismRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129) [Complete proteome] [HAMAP]
Taxonomic identifier266117 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Rubrobacteridae › Rubrobacterales › Rubrobacterineae › Rubrobacteraceae › Rubrobacter

Protein attributes

Sequence length436 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 – 436436Dihydroorotase HAMAP MF_00220_B
PRO_0000325595

Sites

Metal binding661Zinc 1 By similarity
Metal binding681Zinc 1 By similarity
Metal binding1481Zinc 1; via carbamate group By similarity
Metal binding1481Zinc 2; via carbamate group By similarity
Metal binding1851Zinc 2 By similarity
Metal binding2371Zinc 2 By similarity
Metal binding3091Zinc 1 By similarity

Amino acid modifications

Modified residue1481N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1AVY7 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 1278C6F572A4CEC0

FASTA43645,111
        10         20         30         40         50         60 
MSTRSGSAAE LAIRGAHVVD PSSGLDGVTD VVVRGGRVAA VGRGRPAARE LDASGLFLFP 

        70         80         90        100        110        120 
GFVDLHAHWR TPGREDEEDL ESGSSAAAAG GFTGVVMMPN TDPVLDRPAL VSGLVRRAER 

       130        140        150        160        170        180 
ESRVRAFVAA ALHAGLAGER LTEMRLLKEA GALCVSDDGL GTQSAGVLRN GMLYARSAGL 

       190        200        210        220        230        240 
PVILHCEDRT LATGAVHEGA AAALAGVPGT PASAEDVATA AALVLAAETG ARVHITHVST 

       250        260        270        280        290        300 
ALSAALVGFF RGRAAVTADT TPHHTTLTDE LVFALDGLFR VNPPLRPGSD REGVVGALRD 

       310        320        330        340        350        360 
GILDFVATDH APHAPEEKEL PLEEAAPGFL GHETAFAALY TGLVLEGRLS LGRLVEAMSC 

       370        380        390        400        410        420 
GPGRWVGGLG SLSPGSPADL ALVDLGEEWT VSRRTLASRS SNSPYLGRRL RGRVVGTMVG 

       430 
GEMVYDRMGA RLGVRT

« Hide

References

[1]"Complete sequence of Rubrobacter xylanophilus DSM 9941."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S., Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9941 / NBRC 16129.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000386 Genomic DNA. Translation: ABG04441.1.
RefSeqYP_644253.1. NC_008148.1.

3D structure databases

ProteinModelPortalQ1AVY7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1AVY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4116145.
GenomeReviewsGene locus Rxyl_1479 in contig CP000386_GR.
KEGGrxy:Rxyl_1479.
NMPDRfig|266117.6.peg.1361.
PATRIC23369836. VBIRubXyl52678_1517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
OMACDVHPVG.
ProtClustDBCLSK2778564.

Enzyme and pathway databases

BioCycRXYL266117:RXYL_1479-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_RUBXD
AccessionPrimary (citable) accession number: Q1AVY7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 43 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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