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Protein

Phosphoribosylformylglycinamidine synthase subunit PurQ

Gene

purQ

Organism
Caulobacter crescentus (strain NA1000 / CB15N)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.UniRule annotationSAAS annotation

Catalytic activityi

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.UniRule annotationSAAS annotation
L-glutamine + H2O = L-glutamate + NH3.UniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei87 – 871NucleophileUniRule annotation
Active sitei195 – 1951UniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrolase activity Source: UniProtKB-KW
  3. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotation, LigaseUniRule annotationSAAS annotation

Keywords - Biological processi

Purine biosynthesisUniRule annotationSAAS annotation

Keywords - Ligandi

ATP-bindingUniRule annotationSAAS annotation, Nucleotide-binding

Enzyme and pathway databases

BioCyciCAULONA1000:CCNA_02583-MONOMER.
UniPathwayiUPA00074; UER00128.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase subunit PurQUniRule annotationSAAS annotation (EC:6.3.5.3UniRule annotationSAAS annotation)
Short name:
FGAM synthaseUniRule annotation
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase subunit IUniRule annotation
Glutaminase PurQUniRule annotation
Phosphoribosylformylglycinamidine synthase subunit IUniRule annotation
Gene namesi
Name:purQUniRule annotation
Ordered Locus Names:CCNA_02583Imported
OrganismiCaulobacter crescentus (strain NA1000 / CB15N)Imported
Taxonomic identifieri565050 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter
ProteomesiUP000001364: Chromosome

Subcellular locationi

Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Interactioni

Subunit structurei

Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.UniRule annotationSAAS annotation

Protein-protein interaction databases

STRINGi190650.CC_2497.

Structurei

3D structure databases

ProteinModelPortaliB8H040.
SMRiB8H040. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation
Contains glutamine amidotransferase type-1 domain.SAAS annotation
Contains glutamine amidotransferase type-domain.SAAS annotation

Keywords - Domaini

Glutamine amidotransferaseUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiCOG0047.
HOGENOMiHOG000238240.
KOiK01952.
OMAiNPNGSQR.
OrthoDBiEOG6P5ZJP.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_I.
[Graphical view]
PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B8H040-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAAVIVFPG SNCDRDCKVA IERSAGARVE MVWHQETALP DDLDLIVLPG
60 70 80 90 100
GFSYGDYLRC GAMAAQSPVM KEVVSAAGKG VAVVGICNGF QVLTEVGLLP
110 120 130 140 150
GALLRNAGLK YVCKPVELDI VNGQTRFTAG YGEQRQAVMT VGNGEGNYFA
160 170 180 190 200
DEETLDRLEG EGQVVFRYKE NPNGSARDIA GIVNKGGNVL GLMPHPDRAF
210 220
DADLGSEDGA VLFRSIFQSA
Length:220
Mass (Da):23,388
Last modified:March 3, 2009 - v1
Checksum:i0041310F86284C0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001340 Genomic DNA. Translation: ACL96048.1.
RefSeqiYP_002517956.1. NC_011916.1.

Genome annotation databases

EnsemblBacteriaiACL96048; ACL96048; CCNA_02583.
GeneIDi7332933.
KEGGiccs:CCNA_02583.
PATRICi21309709. VBICauCre52860_2533.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001340 Genomic DNA. Translation: ACL96048.1.
RefSeqiYP_002517956.1. NC_011916.1.

3D structure databases

ProteinModelPortaliB8H040.
SMRiB8H040. Positions 2-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190650.CC_2497.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL96048; ACL96048; CCNA_02583.
GeneIDi7332933.
KEGGiccs:CCNA_02583.
PATRICi21309709. VBICauCre52860_2533.

Phylogenomic databases

eggNOGiCOG0047.
HOGENOMiHOG000238240.
KOiK01952.
OMAiNPNGSQR.
OrthoDBiEOG6P5ZJP.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00128.
BioCyciCAULONA1000:CCNA_02583-MONOMER.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
HAMAPiMF_00421. PurQ.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010075. PRibForGlyAmidine_synth_I.
[Graphical view]
PIRSFiPIRSF001586. FGAM_synth_I. 1 hit.
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01737. FGAM_synth_I. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genetic basis of laboratory adaptation in Caulobacter crescentus."
    Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V., Walunas T.L., Crosson S.
    J. Bacteriol. 192:3678-3688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NA1000 / CB15NImported.

Entry informationi

Entry nameiB8H040_CAUCN
AccessioniPrimary (citable) accession number: B8H040
Entry historyi
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: February 4, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

In Gram-negative bacteria and most eukaryotes, FGAM synthase is only formed by PurL, a single polypeptide of 140 kDa (large PurL). However in Gram-positive bacteria and archaebacteria, phosphoribosylformylglycinamidine synthase is composed of three separate proteins: PurL (small PurL), PurQ and PurS.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

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.