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Q8RC55 (PUR9_THETN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:TTE0592
OrganismThermoanaerobacter tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Caldanaerobacter subterraneus subsp. tengcongensis) [Complete proteome] [HAMAP]
Taxonomic identifier273068 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobacter

Protein attributes

Sequence length508 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 – 508508Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192143

Sequences

Sequence LengthMass (Da)Tools
Q8RC55 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 42D2570B57C222A2

FASTA50856,362
        10         20         30         40         50         60 
MSRRALISVS KKDGIVEFAK KLEDLGYEII STGGTYNLLK ESGVKVIKVS EVTGFPEIMG 

        70         80         90        100        110        120 
GRVKTLHPKI HGGILAVRDK KEHLKDLNDH GIVPIDLVAI NLYPFKETIS REKVALEEAI 

       130        140        150        160        170        180 
ENIDIGGPAM IRAAAKNYKY VTVLVDPVDY EKVIEEIKLY GDTKEETRFY LAAKAFGHTA 

       190        200        210        220        230        240 
FYDSLIYEYF REKTNMEFPK VITFAYEKVQ DLRYGENPHQ KAAFYKNPVK SYGIAECLQL 

       250        260        270        280        290        300 
HGKELSFNNI NDANAAIELV REFSEPVAVA IKHTNPCGVA VGNSIYEAYL KAYEADPVSI 

       310        320        330        340        350        360 
FGGIVAFNGK VDVDTAKELV KIFLEIVIAP DFEEEALEIL MSKKNLRVLK LKEGYYREFD 

       370        380        390        400        410        420 
LKKVEGGVLV QQKDEIDLDE SSIKVVTKRA PTGKEMKDLK FAWKVVKHVK SNAIVLAKDG 

       430        440        450        460        470        480 
VTVGIGVGQV NRIWPTEQAI KQAGERAKGS VLASDAFFPF PDVVEAAARG GITAIIQPGG 

       490        500 
SQNDQLSIEA ADRAGIAMIF TGIRHFKH 

« Hide

References

[1]"A complete sequence of the T. tengcongensis genome."
Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R. expand/collapse author list , Wang J., Yu J., Yang H.
Genome Res. 12:689-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15242 / JCM 11007 / NBRC 100824 / MB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008691 Genomic DNA. Translation: AAM23862.1.
RefSeqNP_622258.1. NC_003869.1.

3D structure databases

ProteinModelPortalQ8RC55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273068.TTE0592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM23862; AAM23862; TTE0592.
GeneID996381.
KEGGtte:TTE0592.
PATRIC23895844. VBITheTen82880_0593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMAGIGQADN.
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_THETN
AccessionPrimary (citable) accession number: Q8RC55
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2002
Last modified: May 14, 2014
This is version 72 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