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

B5YLE5 (PUR9_THEYD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:THEYE_A1243
OrganismThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87) [Reference proteome] [HAMAP]
Taxonomic identifier289376 [NCBI]
Taxonomic lineageBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio

Protein attributes

Sequence length522 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 – 522522Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096105

Sequences

Sequence LengthMass (Da)Tools
B5YLE5 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 83323A65C8570910

FASTA52258,100
        10         20         30         40         50         60 
MIKRALISVS DKRGLVDFAK ELDKLGVEIL STGGTAKTLR DSGIKVIDVS QYTGFPEIMD 

        70         80         90        100        110        120 
GRVKTLHPLI HGGILARRDN KEDIEAMERL GIKPIDMVVV NLYPFESVAK KHLSQILQPS 

       130        140        150        160        170        180 
DLNLQAFLEE AIENIDIGGP TLLRASAKNY KDVIVIVDPD DYSSIIEDIK KGSVSIEKKF 

       190        200        210        220        230        240 
ELAKKVFSHT ARYDALIADY FEKISPSGFK KDWTLPLKMT RTLRYGENPH QKAALYALNE 

       250        260        270        280        290        300 
SPSLIDADVL QGKEMSFNNY LDTHSAVLLA TEFSEPVCVI VKHNNPCGVA IGENIHTAYK 

       310        320        330        340        350        360 
KAFECDPVSA FGGIIAFNRV VDKETASEII NTFYEVIVAP DFDKDALEVF ETKKNLRLLR 

       370        380        390        400        410        420 
FPSLSDKIQP SGFDLKRILG GFIVQEWDKV DNEFSQAKVV TKRQPTDEEW KALKFAWKVC 

       430        440        450        460        470        480 
KHIKSNAVVY AKEDRTVGLG IGQTSRVFSA KIGAMHALSS LKGTVVASDG FFPFRDNIDV 

       490        500        510        520 
LAQNGVTSII QPGGSVRDQE VIDAANQYNI AMVFTGIRHF RH 

« Hide

References

[1]"The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51303 / DSM 11347 / YP87.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001147 Genomic DNA. Translation: ACI21021.1.
RefSeqYP_002249060.1. NC_011296.1.

3D structure databases

ProteinModelPortalB5YLE5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING289376.THEYE_A1243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI21021; ACI21021; THEYE_A1243.
GeneID6943286.
KEGGtye:THEYE_A1243.
PATRIC23909503. VBITheYel104483_1215.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycTYEL289376:GH9L-1236-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_THEYD
AccessionPrimary (citable) accession number: B5YLE5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 43 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