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Q97CD7 (PUR5_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:TV0165
ORF Names:TVG0175535
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length338 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 – 338338Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148292

Sequences

Sequence LengthMass (Da)Tools
Q97CD7 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 0AC488696971DEF5

FASTA33837,183
        10         20         30         40         50         60 
MPEVKDGIID RKMQGEFVSS FIRQLKFHRE DFKNIGYIGG FTSLIDMGNF ALSFNNDGVG 

        70         80         90        100        110        120 
TKTMIAEQAN KYDTLGIDCV AMNVNDAITV GSEPIAMVDY LAVRDLNEDI AKQLGNGFNV 

       130        140        150        160        170        180 
GAQIANISIV GGETAVVPEI VNHIDVSGAV IGIVQKNQII TGANIKEGDV IIGLGSSGLH 

       190        200        210        220        230        240 
SNGFTTVRKI ISDNEINLFD NFPGESKKTY EVLLEPTRIY VREILDVMGI IQIKGMANIT 

       250        260        270        280        290        300 
GGGFKNITRM KDMKYVIDDP MEPQNVFVRL MELGNLNYKQ MYEIFNMGTG FVVVIGEDDK 

       310        320        330 
IDFINTLKNR VPLKVIGHVE NGTGVEIPKY SVSLMGYY 

« Hide

References

[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000011 Genomic DNA. Translation: BAB59307.1.
RefSeqNP_110683.1. NC_002689.2.

3D structure databases

ProteinModelPortalQ97CD7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273116.TVN0164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB59307; BAB59307; BAB59307.
GeneID1441650.
KEGGtvo:TVN0164.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
KOK01933.
OMAVIGKIEH.

Enzyme and pathway databases

BioCycTVOL273116:GC31-169-MONOMER.
UniPathwayUPA00074; UER00129.

Family and domain databases

Gene3D3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPMF_00741_A. AIRS_A.
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_THEVO
AccessionPrimary (citable) accession number: Q97CD7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 76 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