Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphoribosylformylglycinamidine cyclo-ligase

Gene

purM

Organism
Streptococcus suis
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.UniRule annotation

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

UniPathwayiUPA00074; UER00129.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine cyclo-ligaseUniRule annotation (EC:6.3.3.1UniRule annotation)
Alternative name(s):
AIR synthaseUniRule annotation
AIRSUniRule annotation
Phosphoribosyl-aminoimidazole synthetaseUniRule annotation
Gene namesi
Name:purMUniRule annotation
OrganismiStreptococcus suis
Taxonomic identifieri1307 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

Cytoplasm UniRule annotation

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 – 340340Phosphoribosylformylglycinamidine cyclo-ligasePRO_0000148265Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9F1T6.
SMRiQ9F1T6. Positions 15-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AIR synthase family.UniRule annotation

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.

Q9F1T6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTNKNAYAQS GVDVEAGYEV VERIKKHVAR TERLGVMGAL GGFGGMFDLT
60 70 80 90 100
KLDVKEPVLV SGTDGVGTKL MLAIQYDKHD TIGQDCVAMC VNDIIAAGAE
110 120 130 140 150
PLYFLDYIAT GKNEPAKLEQ VVAGVAEGCV QAGCGLIGGE TAEMPGMYGE
160 170 180 190 200
DDYDLAGFAV GIAEKYQIID GSKVKEGDIL LGLASSGIHS NGYSLVRRVF
210 220 230 240 250
ADVSGDALLP ELNGRALKDV LLEPTRIYVQ QVLPLVKAGL VNGIAHITGG
260 270 280 290 300
GFIENVPRMF ADNLAAEIEE DKIPVLPIFT ALEKYGKIKH EEMFEIFNMG
310 320 330 340
IGLVLAVSPD KVDSVCQLVD EEVYTIGRII AKEDKSVVIK
Length:340
Mass (Da):36,358
Last modified:March 1, 2001 - v1
Checksum:iE043F5BD1BE19288
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045609 Genomic DNA. Translation: BAB20825.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB045609 Genomic DNA. Translation: BAB20825.1.

3D structure databases

ProteinModelPortaliQ9F1T6.
SMRiQ9F1T6. Positions 15-332.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00074; UER00129.

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. "Evidence for horizontal transfer of the SsuDAT1I restriction-modification genes to the Streptococcus suis genome."
    Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.
    J. Bacteriol. 183:500-511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DAT1 / Serotype 2.

Entry informationi

Entry nameiPUR5_STRSU
AccessioniPrimary (citable) accession number: Q9F1T6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.