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Q88U29 (PUR9_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:lp_2720
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length510 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192097

Sequences

Sequence LengthMass (Da)Tools
Q88U29 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 6054866F95DD0CBA

FASTA51055,306
        10         20         30         40         50         60 
MTKRALLSVS DKQGLTDFAK GLVALDYELI STGGTKKALE AADIPVIGIE EVTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HAGLLARRDL PAHMAQLKAA GIQPIDMVVV NLYPFKATIQ QPDVTQAEAI 

       130        140        150        160        170        180 
EQIDIGGPSM LRSAAKNFAA VLPIVDPADY EQILADLQTD AVTPALRQRL AAKVFQHTAA 

       190        200        210        220        230        240 
YDALIAQYLT TEEFPEKLTL TYDKKQALRY GENSHQKAAF YENALPTHFS ITGAKQIHGK 

       250        260        270        280        290        300 
ELSYNNIKDA DAALRMVSEY QQPAVVAMKH MNPCGVGLGT TIEAAWDKAY EADSISIFGG 

       310        320        330        340        350        360 
IIALNRPVDL ATAEKMHALF LEIIIAPSFD DDAFAILAKK KNLRLMTVDF EQTHTADKFE 

       370        380        390        400        410        420 
TISVGGGLLR QEVDAAFETP ADFTVVTVTQ PTPAQLKALA FGQQVVKHVK SNAVVVTTAD 

       430        440        450        460        470        480 
RTLGIGSGQM NRIDSTKIAI GKAMKQAGYE NAILASDAFF PMDDCVEYAA QHGIRAIVQP 

       490        500        510 
GGSIRDKDSI AMADRYGIAM VTTGVRHFRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC79835.1.
RefSeqYP_004890349.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88U29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_2720.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC79835; CCC79835; lp_2720.
GeneID1063024.
KEGGlpl:lp_2720.
PATRIC22251335. VBILacPla27411_2275.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
ProtClustDBPRK00881.

Enzyme and pathway databases

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_LACPL
AccessionPrimary (citable) accession number: Q88U29
Secondary accession number(s): F9URJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: February 19, 2014
This is version 71 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