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B0SGW3 (PUR9_LEPBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:LBF_1416
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]
Taxonomic identifier355278 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

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_1000096070

Sequences

Sequence LengthMass (Da)Tools
B0SGW3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 301A01BC4D1754A2

FASTA51356,495
        10         20         30         40         50         60 
MIQIKRALVS VSDKTGITEI CSFLTKHGVE ILSTGGTYDA LSKAGIAVKK VDEFTGFPEI 

        70         80         90        100        110        120 
LHGRVKTLHP KIHGGLLGDT TNPDHVKQME SNGIVPITLV IVNLYPFVKT VMKPDVTLED 

       130        140        150        160        170        180 
AIENIDIGGP SMLRSAAKNH KNVVVLTDPK DYESFQNEFT TNNGKISRET AFGYAAKVFS 

       190        200        210        220        230        240 
ETASYDSAIS SYFNKRLGIK YPDKITFAFN KKQKLRYGEN PHQDAAFYEP LFLKSQFEAL 

       250        260        270        280        290        300 
QGKELSFNNM LDFDAAFHVA SLLPKNAVSI VKHLNPCGIA FGETVLESFE LARKTDPISA 

       310        320        330        340        350        360 
FGGIIGIHGR VEKESAEEIT KNFVEGVIAE SFSNEALEIF AKKPNIRLIP IAKFDEALDE 

       370        380        390        400        410        420 
LDLRSLHHGL LIQNRDYDLI TKDKLKIVSK KQPTEDDLEG LMFAWNCVKF IKSNAIVYTD 

       430        440        450        460        470        480 
QNSTLGIGAG QMSRVDSVEL GAMKAQKVGL SVVGSYVGSD AFFPFRDGID AIAKVGAKAI 

       490        500        510 
IQPGGSIRDE EVIQAADEHG LIMVFTGMRH FRH 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / Ames.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000777 Genomic DNA. Translation: ABZ93930.1.
RefSeqYP_001962508.1. NC_010842.1.

3D structure databases

ProteinModelPortalB0SGW3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355278.LBF_1416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ93930; ABZ93930; LBF_1416.
GeneID6387421.
KEGGlbf:LBF_1416.
PATRIC22341881. VBILepBif95142_1502.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLBIF355278:GHTJ-1413-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_LEPBA
AccessionPrimary (citable) accession number: B0SGW3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 44 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