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B2G5C2 (PUR9_LACRJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:LAR_0138
OrganismLactobacillus reuteri (strain JCM 1112) [Complete proteome] [HAMAP]
Taxonomic identifier557433 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length512 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 – 512512Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096069

Sequences

Sequence LengthMass (Da)Tools
B2G5C2 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: ECEC7A2970255506

FASTA51257,033
        10         20         30         40         50         60 
MKRALVSVSD KQNLVPFVKG LVENGFEIIS TGGTKRVLDE AGIETIGIED VTHFPEILDG 

        70         80         90        100        110        120 
RVKTLNPYVH GGLLARRNLP EHMATLEKLN ITPIDLVCVN LYPFKETIEK PGVEIADAIE 

       130        140        150        160        170        180 
NIDIGGPSMV RSAAKNYHDV TIVVDQADYD EVLAQIKEDG ETSLATRARL AAKAFRHTAA 

       190        200        210        220        230        240 
YDSLISQYLT KQTGLEDPEK LTLSWDLKET MRYGENSHQK AWLYEDALPK AFSVLQAKQL 

       250        260        270        280        290        300 
HGKKLSYNNI KDADEALRCI REFDEPTVVA MKHMNPCGIG RGDSLVQAWD RAYEADPVSI 

       310        320        330        340        350        360 
FGGVIALNRQ VDLVTAEKMH KIFLEIVIAP GFDDDAFELL AKKKNIRLLT LDFSKKDEPT 

       370        380        390        400        410        420 
KHEVVSVMGG MLLQEQDMLK EDYHDWQCVT EKQPTEEQLK TLMFAWKAVK HAKSNAIVLA 

       430        440        450        460        470        480 
NDERTLGVGE GQPNRIDSLK IAVKHAGEAI DDRTVMASDA FFPFGDCVEY AGQNGIKAIV 

       490        500        510 
QPGGSVRDQE SIEMANKYGI AMVTTGIRHF RH 

« Hide

References

[1]"Comparative genome analysis of Lactobacillus reuteri and Lactobacillus fermentum reveal a genomic island for reuterin and cobalamin production."
Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T., Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T., Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T., Hattori M.
DNA Res. 15:151-161(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 1112.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007281 Genomic DNA. Translation: BAG24654.1.
RefSeqYP_001841134.1. NC_010609.1.

3D structure databases

ProteinModelPortalB2G5C2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557433.LAR_0138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG24654; BAG24654; LAR_0138.
GeneID6230200.
KEGGlrf:LAR_0138.
PATRIC22257458. VBILacReu111271_0147.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycLREU557433:GHNR-140-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_LACRJ
AccessionPrimary (citable) accession number: B2G5C2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 10, 2008
Last modified: May 14, 2014
This is version 48 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