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C1D6F1 (PUR9_LARHH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 42. 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:LHK_03208
OrganismLaribacter hongkongensis (strain HLHK9) [Complete proteome] [HAMAP]
Taxonomic identifier557598 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeLaribacter

Protein attributes

Sequence length526 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 – 526526Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122962

Sequences

Sequence LengthMass (Da)Tools
C1D6F1 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 82364408DBB769E2

FASTA52656,135
        10         20         30         40         50         60 
MTKIERALIS VSDKTGILEF ARGLAAHGVE ILSTGGTAKL LADNNVPVIE VADYTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KIHGGILGRR DLPEHVAKMA EHGIGNIDLV CVNLYPFEAT IAKEGCALED 

       130        140        150        160        170        180 
AIENIDIGGP TMVRSAAKNW AHVAIVTDAA DYPALLEEMG ANAGALSRAT RFDLSRKAFT 

       190        200        210        220        230        240 
HTAAYDGAIS NYLTAVQADQ GLAGEPVRTL FPTRLNLQVV KVQDMRYGEN PHQSAAFYRD 

       250        260        270        280        290        300 
LDPAPGTLAH YRQLQGKELS YNNIADSDAA WEAVKTFDDP ACVIVKHANP CGVAVAADPL 

       310        320        330        340        350        360 
SAYRLAFATD TTSAFGGIIA FNREVDAATV EAVSAQFLEV LIAPAFTDDA KALIAAKKNV 

       370        380        390        400        410        420 
RVLEVPVEAG ANRFELKRVG GGLLVQTPDI KNVTLDELKV VTKAQPTRQQ LADLLFAWRV 

       430        440        450        460        470        480 
AKFVKSNAIV FAAGGQTAGI GAGQMSRVDS TRIAARKAQD AGLSLKNAVA ASDAFFPFRD 

       490        500        510        520 
GVDVIAEQGI SAIIQPGGSM RDEEVIKAAD EHGIAMVFTG NRHFRH 

« Hide

References

[1]"The complete genome and proteome of Laribacter hongkongensis reveal potential mechanisms for adaptations to different temperatures and habitats."
Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.
PLoS Genet. 5:E1000416-E1000416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLHK9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001154 Genomic DNA. Translation: ACO76186.1.
RefSeqYP_002797195.1. NC_012559.1.

3D structure databases

ProteinModelPortalC1D6F1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557598.LHK_03208.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO76186; ACO76186; LHK_03208.
GeneID7758815.
KEGGlhk:LHK_03208.
PATRIC22303172. VBILarHon49832_2936.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycLHON557598:GHO5-3272-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_LARHH
AccessionPrimary (citable) accession number: C1D6F1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: July 9, 2014
This is version 42 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