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Q051H8 (PUR9_LEPBL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:LBL_1554
OrganismLeptospira borgpetersenii serovar Hardjo-bovis (strain L550) [Complete proteome] [HAMAP]
Taxonomic identifier355276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length511 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 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018905

Sequences

Sequence LengthMass (Da)Tools
Q051H8 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 7FAC8E67BA8A92B9

FASTA51156,137
        10         20         30         40         50         60 
MIQIKRALIS VSDKSDIVEF AQFLNQNGVE IISTGGTLKL LKDNGIQAIA IDDYTGFPEI 

        70         80         90        100        110        120 
LEGRVKTLHP KVHGGLLGVV SNPAHKQKME ELKIPKIDLV VVNLYPFLKT VSKPGVQLEE 

       130        140        150        160        170        180 
AIENIDIGGP SMIRSAAKNY KHTLVLTDPS DYEEVRVLIA SGGISEEVAA GYMRKAFSHT 

       190        200        210        220        230        240 
AMYDTAISSW FHKQAGDVFP DVLNLSFLKK QKLRYGENPH QAASFYEPLF VKSDFSPLQG 

       250        260        270        280        290        300 
KELSFNNMLD FDAAFHISSL LPENTVCIIK HLNPCGIAYA DDPLEAFQLA RRTDPISAFG 

       310        320        330        340        350        360 
GVIGIKGIVH GELATAITEN FVEGVIAQKF TPEALELFSK KPNIRLIEIE NFKEALDELD 

       370        380        390        400        410        420 
LRPIHHGLLI QERDYTTITE KDLKVVTKKQ PTSDDIRGLM FAWSCVRFIK SNAIVYTEEN 

       430        440        450        460        470        480 
ATLGIGAGQM SRVDSVQLGA NKALNVGLSV VGSYVASDAF FPFRDGIDAL AKAGAKAIIQ 

       490        500        510 
PGGSVRDAEV IQAADEHGLI MVFTGMRHFR H 

« Hide

References

[1]"Genome reduction in Leptospira borgpetersenii reflects limited transmission potential."
Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.
Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L550.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000348 Genomic DNA. Translation: ABJ79017.1.
RefSeqYP_797950.1. NC_008508.1.

3D structure databases

ProteinModelPortalQ051H8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355276.LBL_1554.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ79017; ABJ79017; LBL_1554.
GeneID4408268.
KEGGlbl:LBL_1554.
PATRIC22367024. VBILepBor75619_1968.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycLBOR355276:GHUQ-1539-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_LEPBL
AccessionPrimary (citable) accession number: Q051H8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 51 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