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Q7V834 (PURQ_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 72. 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 synthase 1

EC=6.3.5.3
Alternative name(s):
Phosphoribosylformylglycinamidine synthase I
Short name=FGAM synthase I
Gene names
Name:purQ
Ordered Locus Names:PMT_0539
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. HAMAP-Rule MF_00421

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 1/2. HAMAP-Rule MF_00421

Subunit structure

Heterodimer of two subunits, PurQ and PurL By similarity.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00421.

Sequence similarities

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPurine biosynthesis
   Cellular componentCytoplasm
   DomainGlutamine amidotransferase
   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

glutamine metabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoribosylformylglycinamidine synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Phosphoribosylformylglycinamidine synthase 1 HAMAP-Rule MF_00421
PRO_0000100577

Regions

Domain2 – 217216Glutamine amidotransferase type-1

Sites

Active site861Nucleophile By similarity
Active site1941 By similarity
Active site1961 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V834 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3BFCA36A5020997B

FASTA21723,443
        10         20         30         40         50         60 
MSIGVVVFPG SNCDRDVRWA AQGCLNIPTR FLWHETRDLN GLDAVVLPGG FSYGDYLRCG 

        70         80         90        100        110        120 
AIARFAPVLE SLVEFVARGG RVLGICNGFQ VLTELGLLPG ALTRNRSLHF ICEDALLTVE 

       130        140        150        160        170        180 
SNRTPWLMGH QRKDSLTLPI AHGEGRYQCS DETLCQLQDD DAIALRYVNN PNGSVADIAG 

       190        200        210 
ITNKTGNVLG LMPHPERACD PVIGGVDGRG LLQSLLG 

« 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: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20714.1.
RefSeqNP_894372.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V834.
ModBaseSearch...

Protein-protein interaction databases

STRING74547.PMT0539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20714; CAE20714; PMT_0539.
GeneID1727701.
KEGGpmt:PMT0539.
PATRIC23008987. VBIProMar135351_0649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0047.
KOK01952.
OMAVLYRYCS.
ProtClustDBPRK03619.

Enzyme and pathway databases

UniPathwayUPA00074; UER00128.

Family and domain databases

HAMAPMF_00421. PurQ.
InterProIPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_I.
[Graphical view]
PIRSFPIRSF001586. FGAM_synth_I. 1 hit.
TIGRFAMsTIGR01737. FGAM_synth_I. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePURQ_PROMM
AccessionPrimary (citable) accession number: Q7V834
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: October 1, 2003
Last modified: May 29, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families