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

A9AA59 (PUR5_METM6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 47. 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:MmarC6_1419
OrganismMethanococcus maripaludis (strain C6 / ATCC BAA-1332) [Complete proteome] [HAMAP]
Taxonomic identifier444158 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus

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_1000193061

Sequences

Sequence LengthMass (Da)Tools
A9AA59 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 26903857D566BAB5

FASTA34938,145
        10         20         30         40         50         60 
MVTYKDAGVD IYKEDKVIRA LASQIKFERT DAIKPADLKG HYAGAIEFGD YYLVLCTDGV 

        70         80         90        100        110        120 
GSKMVVAEMA NKFDTVPIDM IAMNVNDAIC IGAEPVALVD YMAVEDITED IASQIGKGLN 

       130        140        150        160        170        180 
DGIKESNINL IGGETASLPN MIKGVDLAGT VLAVVKKDEI VSGKEVKPGD VIVGLRSSGI 

       190        200        210        220        230        240 
HSNGLSLARK VFFDITNLDV NSKLSHGKTV AEELLTPTKI YVKPVLEMIK QVNVKGLAHI 

       250        260        270        280        290        300 
TGGGFRKLKR LNKDVCYKID ELPEILPIFK EIQNLGNVAD QEMFKTFNMG IGFCVIVEKE 

       310        320        330        340 
DAEKIIEIAN HHNIPAFVIG KIEDSVEIGG KTKRETVLVE YNNKKMIME 

« Hide

References

[1]"Complete sequence of Methanococcus maripaludis C6."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C6 / ATCC BAA-1332.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000867 Genomic DNA. Translation: ABX02232.1.
RefSeqYP_001549464.1. NC_009975.1.

3D structure databases

ProteinModelPortalA9AA59.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444158.MmarC6_1419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX02232; ABX02232; MmarC6_1419.
GeneID5739143.
KEGGmmx:MmarC6_1419.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229091.
KOK01933.
OMAIDMIAMN.
ProtClustDBPRK05385.

Enzyme and pathway databases

BioCycMMAR444158:GHN2-1465-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_METM6
AccessionPrimary (citable) accession number: A9AA59
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 47 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