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

Q1Q9M0 (PUR5_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 57. 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:Pcryo_1856
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length349 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 – 349349Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000258388

Sequences

Sequence LengthMass (Da)Tools
Q1Q9M0 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 0B06B403F44B0B6C

FASTA34936,863
        10         20         30         40         50         60 
MSNKPSLSYK DAGVDIDAGD ALVQRIKSVA KATSRPEVVG GLGGFGALCR IPTGYTSPLL 

        70         80         90        100        110        120 
VSGTDGVGTK LKLALQLNRH DTIGIDLVAM CVNDLLVCGA EPLFFLDYYA TGKLDVDVAA 

       130        140        150        160        170        180 
TVVTGIGEGC KLSNCALIGG ETAEMPGMYQ DDDYDLAGFC VGVVEEAEVI TGENVAEGDV 

       190        200        210        220        230        240 
LIALASSGAH SNGYSLVRKV IEVSGVDVTS SNEQLDGQSI QDALMAPTRI YVKAIKALQD 

       250        260        270        280        290        300 
TLGSSALHAM SHITGGGLTD NLPRVLPETL AASIDTNSWQ FSELFTWLQN QGNIEQSEMY 

       310        320        330        340 
RTFNCGVGFV IVVPKDKAEA AIQTLNDAGE KAWKLGEMVK READAVVYR 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE75633.1.
RefSeqYP_581117.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1Q9M0.
SMRQ1Q9M0. Positions 6-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_1856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE75633; ABE75633; Pcryo_1856.
GeneID4035190.
KEGGpcr:Pcryo_1856.
PATRIC23063311. VBIPsyCry128170_1971.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPCRY335284:GHE9-1897-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_PSYCK
AccessionPrimary (citable) accession number: Q1Q9M0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 57 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