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A7GH96 (PUR9_CLOBL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:CLI_2931
OrganismClostridium botulinum (strain Langeland / NCTC 10281 / Type F) [Complete proteome] [HAMAP]
Taxonomic identifier441772 [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_1000018877

Sequences

Sequence LengthMass (Da)Tools
A7GH96 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 5994081894D28B50

FASTA49955,775
        10         20         30         40         50         60 
MIKRALISVF DKTGILDLAK FLESRDVEII STGGTYKHLK ENGVKVIDIE EVTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLNPLI HGGILAIRDN EEHMKVIEEK GINPIDMVVV NLYPFFNKVE ENLSFDEKVE 

       130        140        150        160        170        180 
FIDIGGPTMI RAAAKNFKDV VVLTDTKDYE NVIDEIKEND QVNIKTRKKL AGKVFNLMSA 

       190        200        210        220        230        240 
YDAAISNFLL EEEYPEYLTL SYKKNIDLRY GENPHQTAAY YTSTVGKYPM KNFEKLNGKE 

       250        260        270        280        290        300 
LSYNNIKDMD IAWKTVCEFE EVACCALKHN TPCGVAIGDT VQEVYTKAYE CDLISIFGGI 

       310        320        330        340        350        360 
VAFNRKVDKE TAENLAKIFL EIVVAPDFDE DALEVLKNKK NLRVIKCEEK STEGKDMAKV 

       370        380        390        400        410        420 
DGGILVQKSD NKLLEDTKVV TEKSPTEQEM KDLIFGMKVV KYVKSNAIVV VKDGMAKGIG 

       430        440        450        460        470        480 
GGQVNRIWAA KEALDRAGDG VVLASDAFFP FGDVAEEAAK WGIKAIIQPG GSIRDEESIK 

       490 
VCNEKGISMV FTGIRHFKH 

« Hide

References

[1]Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Langeland / NCTC 10281 / Type F.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000728 Genomic DNA. Translation: ABS39608.1.
RefSeqYP_001392156.1. NC_009699.1.

3D structure databases

ProteinModelPortalA7GH96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING441772.CLI_2931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS39608; ABS39608; CLI_2931.
GeneID5405142.
KEGGcbf:CLI_2931.
PATRIC19428817. VBICloBot15611_2850.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADEIACCA.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCBOT441772:GJIE-2895-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_CLOBL
AccessionPrimary (citable) accession number: A7GH96
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 46 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