Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot A4IM31 (PYRC_GEOTN)

Last modified September 2, 2008. Version 16. 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: GTNG_1007
OrganismGeobacillus thermodenitrificans (strain NG80-2) [Complete proteome] [HAMAP]
Taxonomic identifier420246 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length428 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 – 428428Dihydroorotase
PRO_1000024085

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding1431Zinc 1; via carbamate group By similarity
Metal binding1431Zinc 2; via carbamate group By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2331Zinc 2 By similarity
Metal binding3061Zinc 1 By similarity

Amino acid modifications

Modified residue1431N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4IM31-1 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: BD249EB5D54F76BB

FASTA42846,453
        10         20         30         40         50         60 
MAMWLKNGMS FNENGQLVRT HIKIEHGNIA AIHHEQLFEA NGEDVIDVGG KLIAPGLIDV 

        70         80         90        100        110        120 
HVHLREPGGE AKETIETGTL AAAKGGFTTV AAMPNTNPVP DRKEQMEWLA RRIQETAHVR 

       130        140        150        160        170        180 
VLPYASITLG QKGEELTDFA ALKEAGAFAF TDDGVGVQSA GMMFEAMKRA AALDMAIVAH 

       190        200        210        220        230        240 
CEDDTLKNGG AVHDGDFARR YGIAGIPSVC EAVHIARDVL LAEATGCHYH VCHISTKESV 

       250        260        270        280        290        300 
RVVRDAKRAG ICVTAEVTPH HLLLCDEDIP RLDANYKMNP PLRSRADREA LIEGLLDGTI 

       310        320        330        340        350        360 
DFIATDHAPH TAAEKAKGME AAPFGIVGLE TAFPLLYTHF VKKNVFTLKQ LVDWLTIKPA 

       370        380        390        400        410        420 
QCFGLQTGRL EVGAPADITV IDLETEEPID PETFASKGNN TPFAGWRCQG WPVMTFVGGT 


LVWEKGRA 

« Hide

References

[1]"Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed: 17372208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000557 Genomic DNA. Translation: ABO66385.1.
RefSeqYP_001125130.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Genome annotation databases

GeneID4965950.
GenomeReviewsGene locus GTNG_1007 in contig CP000557_GR.
KEGGgtn:GTNG_1007.
NMPDRfig|420246.5.peg.976.

Organism-specific databases

CMRSearch...

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. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_GEOTN
AccessionPrimary (citable) accession number: A4IM31
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: September 2, 2008
This is version 16 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