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Q2RGU9 (PUR9_MOOTA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Moth_2044
OrganismMoorella thermoacetica (strain ATCC 39073) [Reference proteome] [HAMAP]
Taxonomic identifier264732 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella

Protein attributes

Sequence length513 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 – 513513Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018909

Sequences

Sequence LengthMass (Da)Tools
Q2RGU9 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 83F071C4E55605E7

FASTA51354,593
        10         20         30         40         50         60 
MSKRALISVS DKTGLVELAR GLVELGWELL STGGTARTLI AAGLPVTEVA AVTGFPEILD 

        70         80         90        100        110        120 
GRVKTLHPKI HGGILARPTP EHLAQLQEQG IQPIDLVVVN LYPFRETIAR PGVTPAEAIE 

       130        140        150        160        170        180 
NIDIGGPAMV RAAAKNHERV GIVVDPASYN EVLTELREKG SLSPETRRRL AAAAFAHTAA 

       190        200        210        220        230        240 
YDAAIAAYFQ RLMRNEEPFP ASFVLSGEKV QDLRYGENPH QGAAFYRLPA PPPGTLAGAR 

       250        260        270        280        290        300 
QLQGKELSYN NLMDLDAAWN LACDFKEPVV AIIKHTNPCG VARASTPAAA YRLAYAADPV 

       310        320        330        340        350        360 
SAFGGIVACN RPVDGEMAGA MTEIFLEAVI APSFTPEAMA ILKSKSNLRL LAAGERAGCR 

       370        380        390        400        410        420 
TREYQIRPVS GGFLVQEPDY HVLEPESLKV VTARKPEAKE MADLLFAWQV VKHVKSNAIV 

       430        440        450        460        470        480 
VARDGVTLGI GAGQMNRVGA ARIALEQAGA RAKGAVLASD AFFPFGDTVE LAAGAGITAI 

       490        500        510 
IQPGGSIRDE ESIRAADAAG IAMVFTGIRH FRH 

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References

[1]"The complete genome sequence of Moorella thermoacetica (f. Clostridium thermoaceticum)."
Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.
Environ. Microbiol. 10:2550-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39073.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000232 Genomic DNA. Translation: ABC20340.1.
RefSeqYP_430883.1. NC_007644.1.

3D structure databases

ProteinModelPortalQ2RGU9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264732.Moth_2044.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC20340; ABC20340; Moth_2044.
GeneID3831190.
KEGGmta:Moth_2044.
PATRIC22641504. VBIMooThe6753_2220.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycMTHE264732:GH0A-2120-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_MOOTA
AccessionPrimary (citable) accession number: Q2RGU9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 60 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