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A4XKZ4 (PUR5_CALS8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Csac_1994
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length341 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 – 341341Phosphoribosylformylglycinamidine cyclo-ligase HAMAP-Rule MF_00741
PRO_1000083453

Sequences

Sequence LengthMass (Da)Tools
A4XKZ4 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E7BF642BF502BCE1

FASTA34137,171
        10         20         30         40         50         60 
MTTYKDAGVN IEEGYKAVNL IKNIAKETFD SNVITDIGSF GSMYLLNIEN SDYILVSGTD 

        70         80         90        100        110        120 
GVGTKLKIAF YMDKHDTVGI DCVAMCVNDI LCHGAKPLFF LDYIACGKLK SEKVATIVKG 

       130        140        150        160        170        180 
VAEGCKIAGC SLVGGETAEM PGFYREEEYD LAGFAVGLVK KDLAICGQDV KEGDILIGLA 

       190        200        210        220        230        240 
SNGVHSNGYS LVRKVFGIDE NPKVLTKVYE ELNLSLGEEL LKPTRIYVKP VLKVLEKIKI 

       250        260        270        280        290        300 
KGIAHITGGG FFENIPRAFP KGFVAVIEKG TWNILPIFRL IQKYSKVDDN EMFSTFNMGI 

       310        320        330        340 
GMVLIVSKDD VETAMEILNE EGINSYVIGT IEKGEGGVVL R 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43494 / DSM 8903.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP67579.1.
RefSeqYP_001180770.1. NC_009437.1.

3D structure databases

ProteinModelPortalA4XKZ4.
SMRA4XKZ4. Positions 16-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351627.Csac_1994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP67579; ABP67579; Csac_1994.
GeneID5088825.
KEGGcsc:Csac_1994.
PATRIC21253732. VBICalSac56748_2172.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0150.
HOGENOMHOG000229091.
KOK01933.
OMAVIGKIEH.
OrthoDBEOG61CM1V.

Enzyme and pathway databases

BioCycCSAC351627:GJ17-2035-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_CALS8
AccessionPrimary (citable) accession number: A4XKZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: May 14, 2014
This is version 48 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