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Q8FMM3 (PURL_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 62. 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 2

EC=6.3.5.3
Alternative name(s):
Phosphoribosylformylglycinamidine synthase II
Short name=FGAM synthase II
Gene names
Name:purL
Ordered Locus Names:CE2480
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length763 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 MF_00420

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 MF_00420

Subunit structure

Heterodimer of two subunits, PurQ and PurL.

Subcellular location

Cytoplasm By similarity HAMAP MF_00420.

Sequence similarities

Belongs to the FGAMS 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: InterPro

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 763763Phosphoribosylformylglycinamidine synthase 2 HAMAP MF_00420
PRO_0000100451

Regions

Nucleotide binding120 – 13112ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q8FMM3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F50068E33FC109B8

FASTA76380,705
        10         20         30         40         50         60 
MSTIFNDTVE AAAENPDLEQ PYAELGLKDD EYARIKEILG RRPTDAELTV YSVMWSEHCS 

        70         80         90        100        110        120 
YKSSKVHLRY FGETTTPEMA EKILAGIGEN AGVVDIGDGN AVTFRVESHN HPSFVEPHQG 

       130        140        150        160        170        180 
AATGIGGIVR DIMAMGARPI AVMDQLRFGA MDNPDTQRVL PGVVSGISHY GNCLGLPNIG 

       190        200        210        220        230        240 
GETVFDDSYA GNPLVNALAV GTLKVDDLKL AFASGAGNKV MLFGSRTGLD GIGGVSVLGS 

       250        260        270        280        290        300 
ASFEEGEERK LPAVQVGDPF AEKVLIECCL ELYQAGVVVG IQDLGGGGLA CATSELAAAG 

       310        320        330        340        350        360 
DGGMRVNLDA VPLRAEKMSA AEILASESQE RMCAVVTPEN VEKFKQICAK WDVTVAEIGE 

       370        380        390        400        410        420 
VTDEKDRYLV VHNGQTVIDA PASTIDEGPV YNRPVERPAN QDEIQTLGGL ERPDTAEGIR 

       430        440        450        460        470        480 
DAWFKLVSSP ALCSRAFITE QYDRYVRGNT VQAKDANAGV LRIDEETNRG VAISADASGR 

       490        500        510        520        530        540 
YTRLDPRTGA RLALAEAYRN VVSTGARPVA VTNCLNFGSP ENAGVMWQFK EAVHGLADGA 

       550        560        570        580        590        600 
KEMGIPVSGG NVSFYNQTGD EPILPTPVVG VLGVLDDVEK TIGNRLPAGE QELYLLGETL 

       610        620        630        640        650        660 
DEFGGSIWQQ VSGAGLSGLP PQIDLANEQR LADLLVPAAD LVGAAHDLSE GGLGQTLAEL 

       670        680        690        700        710        720 
AIHAGRGLDV DLTQVHEDLF TALFSESASR IVVATTRGDE LVARAQELGV PVTRLGVTND 

       730        740        750        760 
SGVITVRGGD LSVEVSVEEL HDAWSNTLPE AFGHAVGANS VVE 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC19290.1.
RefSeqNP_739090.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FMM3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1032100.
GenomeReviewsGene locus CE2480 in contig BA000035_GR.
KEGGcef:CE2480.
NMPDRfig|196164.1.peg.2480.
PATRIC21491107. VBICorEff9312_2448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG311214.
OMAYGNSFGV.
PhylomeDBQ8FMM3.
ProtClustDBPRK01213.

Enzyme and pathway databases

BioCycCEFF196164:CE2480-MONOMER.

Family and domain databases

HAMAPMF_00420. PurL_2.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR010074. PRibForGlyAmidine_synth_II.
IPR016188. PurM_N-like.
[Graphical view]
KOK01952.
PfamPF00586. AIRS. 2 hits.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMSSF56042. AIR_synth_C. 2 hits.
SSF55326. PurM_N-like. 2 hits.
TIGRFAMsTIGR01736. FGAM_synth_II. 1 hit.
ProtoNetSearch...

Entry information

Entry namePURL_COREF
AccessionPrimary (citable) accession number: Q8FMM3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 62 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