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Q7UZR7 (PUR5_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:PMM1589
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length347 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 – 347347Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_0000148232

Sequences

Sequence LengthMass (Da)Tools
Q7UZR7 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 6AB0B5082C9A9E47

FASTA34738,869
        10         20         30         40         50         60 
MDYKTSGVDI KAGREFVSEI KQSVESTYSS NVLEGIGGFG GLFKIPLEGL KKPVLVSGTD 

        70         80         90        100        110        120 
GVGTKLELAQ IKNFHFEVGI DLVAMCMNDI ITTGAKPLFF LDYIATGKLE KNQLLEVING 

       130        140        150        160        170        180 
IAHSCRENKC SILGGETAEM PGFYSKNKYD LAGFCVGIAD EEKLINGKKI CENDLIIALQ 

       190        200        210        220        230        240 
SNGMHSNGFS LVRKIIENNN QIDKQFEKKY NLDFYDELLK PTKIYFKIVN QILSQNIQIK 

       250        260        270        280        290        300 
GMSHITGGGI PENLPRCMSS DFIPYIDKKS WKIPVLFEFL KDVGQIPEKD FWNTFNLGVG 

       310        320        330        340 
FCLIIDKKYK DKILNICNAF DISSWVLGKV LKKNNSKENN FLPEIII 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE20048.1.
RefSeqNP_893706.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7UZR7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM1589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20048; CAE20048; PMM1589.
GeneID1726365.
KEGGpmm:PMM1589.
PATRIC23034362. VBIProMar68066_1830.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229090.
KOK01933.
OMACFEIPAG.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-1633-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_PROMP
AccessionPrimary (citable) accession number: Q7UZR7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 71 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