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P46534 (PYRE_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 60. 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:
Orotate phosphoribosyltransferase

Short name=OPRT
Short name=OPRTase
EC=2.4.2.10
Gene names
Name:pyrE
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity. HAMAP MF_01208

Catalytic activity

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208

Cofactor

Magnesium By similarity. HAMAP MF_01208

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208

Subunit structure

Homodimer By similarity. HAMAP MF_01208

Induction

Repressed by uracil. Ref.1

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_0000110666

Regions

Region119 – 12795-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site9315-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site9715-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site9915-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1231Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
P46534 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 72FDD9B0419335E0

FASTA20622,402
        10         20         30         40         50         60 
MKHDIAAKLL QIGAVALQPN EPFTWSSGLK SPIYCDNRLT LAYPGVRRLI ADALAELIRT 

        70         80         90        100        110        120 
HFPKADLIAG TAAGIPHAAW VSERLELPMC YVRSQAKRHG KGKQIEGQAR PGQRVVVIED 

       130        140        150        160        170        180 
LISTGGTSLA AVRALKEAGC EVLGVAAIFT YGLEKAKQAF AAENLPAYTL TDYNTLIETA 

       190        200 
VRLGAVSEHD LATLRQWREN PEEWGS 

« Hide

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], INDUCTION.
Strain: DSM 405 / NBRC 15313 / YP-T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73308 Genomic DNA. Translation: CAA51743.1.
PIRI40173.

3D structure databases

ProteinModelPortalP46534.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_01208. PyrE.
[Tree]
InterProIPR004467. Or_phspho_trans_clade-1.
IPR023031. Orotate_PribosylTferase.
IPR000836. PRibTrfase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. PyrE. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRE_BACCL
AccessionPrimary (citable) accession number: P46534
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: September 21, 2011
This is version 60 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