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

C6DBR0 (PUR5_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 33. 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:PC1_1129
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

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_1000212828

Sequences

Sequence LengthMass (Da)Tools
C6DBR0 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 248CD316F92BE04E

FASTA34536,825
        10         20         30         40         50         60 
MTDKTSLSYK DAGVDIDAGN ALVDRIKGVV KQTRRPEVMG GLGGFGALCA LPQKYREPIL 

        70         80         90        100        110        120 
VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAA 

       130        140        150        160        170        180 
SVITGIAEGC KQSGCALVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVQNGDV 

       190        200        210        220        230        240 
LVALASSGPH SNGYSLVRKV LEVSKTDPEQ FELEGKPLAD HLLAPTKIYV KSILSLIEKV 

       250        260        270        280        290        300 
DVHAISHLTG GGFWENIPRV LPEGMQATID ESSWQWPAVF NWLQQAGNVS RHEMYRTFNC 

       310        320        330        340 
GVGMIIALPA EQADEAVALL NSSGENAWKI GVITQTDAGD AVVIN 

« Hide

References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001657 Genomic DNA. Translation: ACT12177.1.
RefSeqYP_003016713.1. NC_012917.1.

3D structure databases

ProteinModelPortalC6DBR0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561230.PC1_1129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT12177; ACT12177; PC1_1129.
GeneID8132058.
KEGGpct:PC1_1129.
PATRIC20486852. VBIPecCar70489_1127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMAIDMIAMN.
OrthoDBEOG61CM1V.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycPCAR561230:GKCK-1159-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_PECCP
AccessionPrimary (citable) accession number: C6DBR0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 33 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