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

Q2IQE7 (PUR5_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. 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:
Phosphoribosylformylglycinamidine cyclo-ligase

EC=6.3.3.1
Alternative name(s):
AIR synthase
AIRS
Phosphoribosyl-aminoimidazole synthetase
Gene names
Name:purM
Ordered Locus Names:Adeh_1255
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP-Rule MF_00741

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP-Rule MF_00741

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00741.

Sequence similarities

Belongs to the AIR synthase family.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine cyclo-ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258326

Sequences

Sequence LengthMass (Da)Tools
Q2IQE7 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: B436F7CF742A231C

FASTA34536,501
        10         20         30         40         50         60 
MSLTYRDAGV DIDEGDRLVD LIKPHARPTL RPEVLGGIGG FGGLFALDVK KYREPVLVSG 

        70         80         90        100        110        120 
TDGVGTKLKV AFAADRHDTV GIDLVAMCVN DIAVVGAEPL FFLDYYATGK LSAEQGAEVV 

       130        140        150        160        170        180 
KGIAEGCRQA GCALIGGETA ELPGFYARGE YDLAGFAVGC VDRPRIVDGT RVARGDVVIG 

       190        200        210        220        230        240 
IASSGLHSNG FSLARKALLD RYPLDHRFEG LGGRTLADAL LEPTRIYAKD VLALLDQVPV 

       250        260        270        280        290        300 
RAFAHITGGG LPGNVPRTLP DGTRAVLEEK RWPRPAIFDV VEREGQVPRD EMYRTFNMGL 

       310        320        330        340 
GLVAVVAPGD EAAAHAALRA RGLEAWTVGA IEAGGPGEAT CEVVR 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC81029.1.
RefSeqYP_464466.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IQE7.
SMRQ2IQE7. Positions 1-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290397.Adeh_1255.

Proteomic databases

PRIDEQ2IQE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC81029; ABC81029; Adeh_1255.
GeneID3888824.
KEGGade:Adeh_1255.
PATRIC20918619. VBIAnaDeh31384_1300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAHCVNDIL.
OrthoDBEOG61CM1V.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycADEH290397:GI2Z-1271-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00741_B. AIRS_B.
InterProIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_ANADE
AccessionPrimary (citable) accession number: Q2IQE7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 58 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