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Reviewed, UniProtKB/Swiss-Prot Q1QVP5 (PUR5_CHRSD)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoribosylformylglycinamidine cyclo-ligase
    EC=6.3.3.1
Alternative name(s):
    AIRS
    Phosphoribosyl-aminoimidazole synthetase
    AIR synthase
Gene names
Name: purM
Ordered Locus Names: Csal_2112
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00741

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5. HAMAP MF_00741

Subcellular location

Cytoplasm By similarity.

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: InterPro

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Phosphoribosylformylglycinamidine cyclo-ligase HAMAP MF_00741
PRO_0000258346

Sequences

Sequence LengthMass (Da)Tools
Q1QVP5-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: BFEAEF3A2DC47866

FASTA35837,887
        10         20         30         40         50         60 
MTRSSDTPSS SRASLSYKDA GVDIDAGNAL VERIKGVAKR TSRPEVMGGL GGFGALCQLP 

        70         80         90        100        110        120 
TGYREPVLVS GTDGVGTKLR LAMDLARHDT IGIDLVAMCV NDLVVAGAEP LFFLDYYATG 

       130        140        150        160        170        180 
KLDVDIAADV VTGIGEGCAQ AGCALIGGET AEMPGMYAGS DYDLAGFCVG VVEKSEILDG 

       190        200        210        220        230        240 
SRVAEGDVLL GLASSGPHSN GYSLIRKIIE RGQADLEQEI DGIPLRDALL APTRIYVKSL 

       250        260        270        280        290        300 
LSLIKESDVT VHALSHITGG GLLENVPRVL PDTLAARIDA ASWTRPAVFD WLQREGNVDE 

       310        320        330        340        350 
HEMHRVLNCG IGMVVVVPAA QAERAQAALE AAGETVHRLG EIVPRQDEEE QVRLENVR 

« Hide

References

[1]"Complete sequence of Chromohalobacter salexigens DSM 3043."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000285 Genomic DNA. Translation: ABE59463.1.
RefSeqYP_574162.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4029257.
GenomeReviewsGene locus Csal_2112 in contig CP000285_GR.
KEGGcsa:Csal_2112.
NMPDRfig|290398.4.peg.2128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1QVP5.
OMAQ1QVP5. MAENAYS.

Enzyme and pathway databases

BioCycCSAL290398:CSAL_2112-MON.

Family and domain databases

HAMAPMF_00741.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR004733. PurM_cligase.
[Graphical view]
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR00878. purM. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR5_CHRSD
AccessionPrimary (citable) accession number: Q1QVP5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents