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A5N0Q0 (PUR9_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:CKL_2684
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length499 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 – 499499Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076479

Sequences

Sequence LengthMass (Da)Tools
A5N0Q0 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: C01A33D8D18AD82A

FASTA49955,653
        10         20         30         40         50         60 
MINRALISVY NKEGLLELAQ FLKNKGVELI STGGTYKYLE QNDIQVTEVS KITGFDEILD 

        70         80         90        100        110        120 
GRVKTLHPVI HSGILAKRDN KEHMDTIAKK DILPIDMVVV NLYPFFDKVD DNITFEEKVE 

       130        140        150        160        170        180 
FIDIGGPTMI RAAAKNFKDV IVVTDVGDYS KLIEEIDSKG DVPYDFRKKL AGKVFNLMSA 

       190        200        210        220        230        240 
YDGAISNFLL EEDYPEYLSL SYKKMDNLRY GENPHQSAAY YTATAGTAPM KDFTQLNGKQ 

       250        260        270        280        290        300 
LSYNNIKDMD IAWKVVNEFE EICCVAVKHN TPCGVALGKD LYEAYVKTYE CDPTSIFGGI 

       310        320        330        340        350        360 
IAVNRKLDVK TAEEISKIFV EIVIAPDFDE EALKVLMEKK NLRIIKCSVK PTNSMEIAKV 

       370        380        390        400        410        420 
DGGILVQSAD DKLVENMEVV TDKKPSKEEI NNLIFGMKVC KYVKSNAIVV VKDFMAKGIG 

       430        440        450        460        470        480 
GGQVNRIWPT CHALDRAGDG VVLASDAFFP FNDVVCEAAK YGIKAIIQPG GSVRDKDSIE 

       490 
ECNKNGISMV FTGVRHFKH 

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000673 Genomic DNA. Translation: EDK34696.1.
RefSeqYP_001396067.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N0Q0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING431943.CKL_2684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEDK34696; EDK34696; CKL_2684.
GeneID5390659.
KEGGckl:CKL_2684.
PATRIC19466907. VBICloKlu111549_2788.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCKLU431943:GJF1-2677-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_CLOK5
AccessionPrimary (citable) accession number: A5N0Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 53 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