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Reviewed, UniProtKB/Swiss-Prot P46538 (PYRC_BACCL)

Last modified January 20, 2009. Version 59. 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

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Names and origin

Protein namesRecommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220

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. HAMAP MF_00220

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Dihydroorotase HAMAP MF_00220
PRO_0000147227

Sites

Metal binding601Zinc 1 By similarity
Metal binding621Zinc 1 By similarity
Metal binding1421Zinc 1; via carbamate group By similarity
Metal binding1421Zinc 2; via carbamate group By similarity
Metal binding1791Zinc 2 By similarity
Metal binding2321Zinc 2 By similarity
Metal binding3051Zinc 1 By similarity

Amino acid modifications

Modified residue1421N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P46538-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 759A2AA99F733F4E

FASTA42746,048
        10         20         30         40         50         60 
MGVWLKNGMS FNKDGELMRT HIKIEHGTIA AILYEQPLEA NEDVIDVGGR LIVPGLIDLH 

        70         80         90        100        110        120 
VHLREPGGEA KETIETGTLA AAKGGFTTVA AMPNTNPAPD RKEQMEWLQA RIRETARVNV 

       130        140        150        160        170        180 
LPYAAITIGQ KGEELTDFAA LKEAGAFAFT DDGVGVQSAG MMFEAMKQAA ALDMAIVAHC 

       190        200        210        220        230        240 
EDDTLTNGGA VHDGEFARRY GLRGIPSVCE AVHIARDVLL AEAAGCHYHV CHISTKESVR 

       250        260        270        280        290        300 
VVRDAKRAGI RVTAEVTPHH LLLCDEDIPG LDANYKMNPP LRSREDRDAL IEGLLDGTID 

       310        320        330        340        350        360 
FIATDHAPHT AAEKAKGIEA APFGIVGLET AFPLLYTHFV KTGVFTLKQL VDWLTIKPAQ 

       370        380        390        400        410        420 
CFGLKAGRLA VGAPADIAVI DLETEEAIDP ETFASKGKNT PFAGWVCQGW PVMTFVGGTL 


VWEKGRA

« Hide

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References

[1]"Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus."
Ghim S.Y., Nielsen P., Neuhard J.
Microbiology 140:479-491(1994) [PubMed: 7516791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 405 / IFO 15313 / YP-T.

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Cross-references

Sequence databases

X73308 Genomic DNA. Translation: CAA51737.1.
PIRI40167.

3D structure databases

HSSPHSSP built from PDB template 1GKR based on UniProtKB P81006.
ModBaseSearch...

Protein family/group databases

MEROPSM38.972.

Enzyme and pathway databases

BRENDA3.5.2.3. 1670.

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...

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Entry information

Entry namePYRC_BACCL
AccessionPrimary (citable) accession number: P46538
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 20, 2009
This is version 59 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)

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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