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A4XKT2 (PYRC_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:Csac_1932
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length430 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 – 430430Dihydroorotase HAMAP MF_00220_B
PRO_0000325590

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
A4XKT2 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 75C5C16A7ED4318E

FASTA43047,394
        10         20         30         40         50         60 
MILIKNAQII NSLHDKVEKA DILIVDDKIK KIGKDIEENP EKMTIIDASG KVVMPSFTDI 

        70         80         90        100        110        120 
HCHLREPGFE YKEDIKSGSR SAAAGGFTTI CCMPNTNPPV DNRAMVAYIK YRAREVSPIE 

       130        140        150        160        170        180 
VLPVGAITKG LLGEELAEIG FMKEEGAIAI SDDGKCVMNA NLMKNALLYS RDFSIPVISH 

       190        200        210        220        230        240 
CEDTNLSEGG QINLGYVSTI TGLRGIPREA ESVIIARDIL LAKETKSHLH ITHVSTKESV 

       250        260        270        280        290        300 
RLIKMAKEWG VNVTADTCPH YISLTEEEVL GFNTNAKVNP PLRTQEDVEA LIEGLKEGVI 

       310        320        330        340        350        360 
DCISTDHAPH HKDEKNVEFN LAASGTIGFE TAFSVLFTYL VEKNGFDIGK IVELLNHNPR 

       370        380        390        400        410        420 
KIIGLSPNVL KEGEKANLVI VDLKKKWEVK EENIVSKSKN SVFLGKLLTS YVETVIYNGK 

       430 
ILKKDGVLNC 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
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., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67517.1.
RefSeqYP_001180708.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XKT2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4XKT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5089294.
GenomeReviewsGene locus Csac_1932 in contig CP000679_GR.
KEGGcsc:Csac_1932.
PATRIC21253612. VBICalSac56748_2112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
OMASHHQPHE.
ProtClustDBCLSK2473347.

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_CALS8
AccessionPrimary (citable) accession number: A4XKT2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: May 29, 2007
Last modified: December 14, 2011
This is version 33 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