Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6NID8 (PUR9_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:DIP0839
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length525 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 – 525525Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096057

Sequences

Sequence LengthMass (Da)Tools
Q6NID8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FE36CC0946E9A82D

FASTA52555,796
        10         20         30         40         50         60 
MSDDRKQIKR ALISVYDKTG LEDLARALND AGVEIVSTGS TAAKIADLGV PVTPVEQLTG 

        70         80         90        100        110        120 
FPECLEGRVK TLHPMVHAGI LADTRKEDHL KQLDELNVAP FQLVVVNLYP FTQTVASGAD 

       130        140        150        160        170        180 
FDACVEQIDI GGPSMVRAAA KNHPSVAVVV SPSRYSEIIA AVGNGGFTRA ERTALAVDAF 

       190        200        210        220        230        240 
RHTASYDVAV ATWMGEQIAD ADKPFAEWIG ASYERANILR YGENPHQAAA LYTDPAAPAG 

       250        260        270        280        290        300 
LAQATQLHGK EMSYNNYTDS DAAWRAAWDH ERPCVAIIKH ANPCGIAVSD VSIAEAHRTA 

       310        320        330        340        350        360 
HACDPVSAFG GVIASNREVS VDMAKQVSEI FTEVIIAPSY EDGAVDILSQ KKNIRILVAP 

       370        380        390        400        410        420 
QPQRDELEQR QISGGVLVQR RDLVDAEGDT PANWTLAAGE GASEELLAEL EFAWRAVRAV 

       430        440        450        460        470        480 
KSNAILLAQG GATVGVGMGQ VNRVDAAKLA VERANSLAGD EQRAKGSVAA SDAFFPFADG 

       490        500        510        520 
FEVLAQAGVR AVVQPGGSIR DAEVIEAANK AGVTMYLTGA RHFAH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248356 Genomic DNA. Translation: CAE49355.1.
RefSeqNP_939203.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NID8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP0839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE49355; CAE49355; DIP0839.
GeneID2649301.
KEGGcdi:DIP0839.
PATRIC21482849. VBICorDip47633_0820.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAHRRAHAC.
OrthoDBEOG6QCDFF.

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_CORDI
AccessionPrimary (citable) accession number: Q6NID8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 69 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