Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q74FJ9 (PUR9_GEOSL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. 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
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:GSU0609
OrganismGeobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) [Reference proteome] [HAMAP]
Taxonomic identifier243231 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter ›

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057897

Sequences

Sequence LengthMass (Da)Tools
Q74FJ9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FFB0C16E7098E0A2

FASTA52155,966
        10         20         30         40         50         60 
MAKITRALIS VSDKTGILDF ARELAGYGVE ILSTGGTAKL LRDAGLAVKD VSDFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGMR SNPDHVATMK AHGIEPIDLV VVNLYPFEAT VAKPECTLED 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNN ADVTVLVDPA DYRPVLDEMK ASGGAVSRET NFCLAVKVYQ 

       190        200        210        220        230        240 
HTAAYDGAIS NWLGARTGEG IAAYPDTVTL QFRKAQEMRY GENPHQGAAF YVERQVKEAS 

       250        260        270        280        290        300 
VATARQLQGK ELSYNNIADT DAALECVKQF AEGPACVIVK HANPCGVAVG GTLLEAYDRA 

       310        320        330        340        350        360 
YATDPESAFG GIIAFNRELD ADTARAICDR QFVEVIIAPA VSPEATEVVA AKKNVRLLEC 

       370        380        390        400        410        420 
GTWPEKQQPR LDLKRVNGGI LVQDTDLDLY AELKVVTKRQ PTEQEMKDLL FAWRVAKFVK 

       430        440        450        460        470        480 
SNAIVYGKGN MTIGVGAGQM SRVNSARIAA IKAEHAGLEV KGAVMASDAF FPFRDGIDNA 

       490        500        510        520 
AAVGITAVIQ PGGSMRDAEV IAAADEHGMA MVFTGMRHFR H

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017180 Genomic DNA. Translation: AAR33940.1.
RefSeqNP_951667.1. NC_002939.5.

3D structure databases

HSSPHSSP built from PDB template 1PKX based on UniProtKB P31939.
ProteinModelPortalQ74FJ9.
ModBaseSearch...

Protein-protein interaction databases

STRING243231.GSU0609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAR33940; AAR33940; GSU0609.
GeneID2685298.
KEGGgsu:GSU0609.
PATRIC22023971. VBIGeoSul17553_0608.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycGSUL243231:GH27-602-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]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_GEOSL
AccessionPrimary (citable) accession number: Q74FJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents