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Q1G9G2 (PUR9_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Ldb1436
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 513513Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018898

Sequences

Sequence LengthMass (Da)Tools
Q1G9G2 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 275DF1135A5B8703

FASTA51356,628
        10         20         30         40         50         60 
MKRALVSVSD KNNLVPFVKG LVANDYEIVS TGGTKRVLDE AGIPTISVED VTGFPEILDG 

        70         80         90        100        110        120 
RVKTLNPYIH GGLLARRELP EHVATLKEHK ITPIDLVCVN LYPFKQTIEK PDVTLAEAIE 

       130        140        150        160        170        180 
NIDIGGPSMV RSASKNYRDV TIVVDQADYD QVLAEIEKDG STSLETRARL AAKAFRLTAS 

       190        200        210        220        230        240 
YDALISQYLT EKAGETAPEK LTLTYDLKEA MRYGENSHQK AWLYEDALPK AFSVLQAEQL 

       250        260        270        280        290        300 
NGKELSYNNI KDADEALRCV REFSKPTVVA MKHMNPCGIG QGNTLEEAWD RAYVADPVSI 

       310        320        330        340        350        360 
FGGVIALNRK VDLATAEKMH KIFLEIIIAP DYDEDALAAL KTKKKNLRIL KLDFSKKDEA 

       370        380        390        400        410        420 
TSKETVSVMG GLLVQDQDVL DEDFADWECV TEAKPTQEQL ESLLFAWKAV KHTKSNAIVV 

       430        440        450        460        470        480 
ANNERTLGVG AGQPNRIDSE KIAIDHAAEA LDDRAVLASD AFFPFSDCVE YAGKHGIKAI 

       490        500        510 
VQPGGSVRDQ ESIDMANKYG IAMVFTGVRH FRH 

« Hide

References

[1]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954253 Genomic DNA. Translation: CAI98237.1.
RefSeqYP_619278.1. NC_008054.1.

3D structure databases

ProteinModelPortalQ1G9G2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390333.Ldb1436.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI98237; CAI98237; Ldb1436.
GeneID4085123.
KEGGldb:Ldb1436.
PATRIC22218342. VBILacDel123523_1289.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycLDEL390333:GIXG-1418-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_LACDA
AccessionPrimary (citable) accession number: Q1G9G2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: May 14, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways