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Protein

Phosphoribosylformylglycinamidine cyclo-ligase

Gene

purM

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphoribosylformylglycinamidine cyclo-ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLINT267671:GHQI-1122-MONOMER.
UniPathwayiUPA00074; UER00129.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine cyclo-ligase (EC:6.3.3.1)
Alternative name(s):
AIR synthase
AIRS
Phosphoribosyl-aminoimidazole synthetase
Gene namesi
Name:purM
Ordered Locus Names:LIC_11123
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Taxonomic identifieri267671 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
ProteomesiUP000007037: Chromosome I

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Phosphoribosylformylglycinamidine cyclo-ligasePRO_0000148219Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi267671.LIC11123.

Structurei

3D structure databases

ProteinModelPortaliQ72T98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AIR synthase family.Curated

Phylogenomic databases

KOiK01933.
OMAiNHCVNDI.
OrthoDBiEOG61CM1V.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_00741. AIRS.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMiSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00878. purM. 1 hit.

Sequencei

Sequence statusi: Complete.

Q72T98-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEKITYKNA GVDTEKGREF IQKIKRNVES THGPRVIGGL GGFAGAYDVS
60 70 80 90 100
VLKKYKHPIL LSGTDGVGTK IELARLLKIY NTIGIDLVAM CVNDILVCGG
110 120 130 140 150
EPFFFLDYIA CGKLDPEKMD QIVSGIVQGC KMSNASLLGG ETAEHPGTMK
160 170 180 190 200
EDEFDLAGFV VGAVEKDSMI DGSTIRSGDK ILGLESSGPH SNGFSLIRKL
210 220 230 240 250
LLKEGKYLPT DPQQVKFLKD YALKPTRIYV SSILKLLQQV SVKGMVHITG
260 270 280 290 300
GGYQENIPRI LPQGTQSKFF KEKIPSGYFF EKIKKDHKIE ELELFATFNM
310 320 330 340
GIGYMVIVSE ENAELAKKIM ESSGEVVHEI GEIVSGNKEE VQFV
Length:344
Mass (Da):37,809
Last modified:August 30, 2005 - v2
Checksum:iC97753E386965A4E
GO

Sequence cautioni

The sequence AAS69730.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA. Translation: AAS69730.1. Different initiation.
RefSeqiYP_001093.1. NC_005823.1.

Genome annotation databases

EnsemblBacteriaiAAS69730; AAS69730; LIC_11123.
GeneIDi2769762.
KEGGilic:LIC11123.
PATRICi22374445. VBILepInt6257_1391.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA. Translation: AAS69730.1. Different initiation.
RefSeqiYP_001093.1. NC_005823.1.

3D structure databases

ProteinModelPortaliQ72T98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267671.LIC11123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS69730; AAS69730; LIC_11123.
GeneIDi2769762.
KEGGilic:LIC11123.
PATRICi22374445. VBILepInt6257_1391.

Phylogenomic databases

KOiK01933.
OMAiNHCVNDI.
OrthoDBiEOG61CM1V.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00129.
BioCyciLINT267671:GHQI-1122-MONOMER.

Family and domain databases

Gene3Di3.30.1330.10. 1 hit.
3.90.650.10. 1 hit.
HAMAPiMF_00741. AIRS.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
SUPFAMiSSF55326. SSF55326. 1 hit.
SSF56042. SSF56042. 1 hit.
TIGRFAMsiTIGR00878. purM. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis."
    Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S.
    , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.
    J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fiocruz L1-130.

Entry informationi

Entry nameiPUR5_LEPIC
AccessioniPrimary (citable) accession number: Q72T98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: January 7, 2015
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.