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C6E5Z3 (PUR9_GEOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:GM21_3524
OrganismGeobacter sp. (strain M21) [Complete proteome] [HAMAP]
Taxonomic identifier443144 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length520 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 – 520520Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000203250

Sequences

Sequence LengthMass (Da)Tools
C6E5Z3 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 47CBE06BC7AB9135

FASTA52056,072
        10         20         30         40         50         60 
MAKIGRALIS VSEKTGVVEF SRALAGYGVE ILSTGGTAKL LREAGIAVKD VSEFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGILGMR ENPAHVAKMQ EHGIEPIDMV VVNLYPFEAT VAKEDCTMED 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNN RDVTVVVDHA DYAVVLDEMK NSGGSVSCET NFRLAVKVYQ 

       190        200        210        220        230        240 
HTAAYDGAIS NWLGARTGDG VAAFPDTLTL QYKLAQGMRY GENPHQSGAF YVEKGSKEAS 

       250        260        270        280        290        300 
ISTARQIQGK ELSYNNIGDT DAALECVKQF TEPACVIVKH ANPCGVALGA NIMEAYDKAY 

       310        320        330        340        350        360 
KTDPESSFGG IIAFNRELDE STARAIVERQ FVEVIIAPKV TEAASEVVAA KKNVRLMECG 

       370        380        390        400        410        420 
FWPENPAPRF DYKRVNGGML VQDADLELFT ELKVVTKRAP TDKEMEDLLF TWRVAKFVKS 

       430        440        450        460        470        480 
NAIVYGRDNS TVGVGAGQMS RVNSARIAAI KAEHAGIPVQ GAVMASDAFF PFRDGLDNAA 

       490        500        510        520 
AVGVTAVIQP GGSMRDAEVI AAADEHGIAM VFTAMRHFRH 

« Hide

References

[1]"Complete sequence of Geobacter sp. M21."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Lovley D.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001661 Genomic DNA. Translation: ACT19545.1.
RefSeqYP_003023303.1. NC_012918.1.

3D structure databases

ProteinModelPortalC6E5Z3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING443144.GM21_3524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT19545; ACT19545; GM21_3524.
GeneID8138896.
KEGGgem:GM21_3524.
PATRIC22021496. VBIGeoSp56140_3440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycGSP443144:GHKM-3598-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_GEOSM
AccessionPrimary (citable) accession number: C6E5Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 37 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