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Protein

N5-carboxyaminoimidazole ribonucleotide mutase

Gene

purE

Organism
Acetobacter aceti
Status
Unreviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).UniRule annotation

Catalytic activityi

5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.UniRule annotation

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. N5-carboxyaminoimidazole ribonucleotide synthase (purK), N5-carboxyaminoimidazole ribonucleotide synthase (purK)
  2. N5-carboxyaminoimidazole ribonucleotide mutase (purE), N5-carboxyaminoimidazole ribonucleotide mutase (purE)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei30SubstrateUniRule annotation1
Binding sitei33SubstrateUniRule annotation1
Binding sitei60SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomeraseUniRule annotation
Biological processPurine biosynthesisUniRule annotation

Enzyme and pathway databases

BRENDAi5.4.99.18 33
UniPathwayi
UPA00074;UER00943

Names & Taxonomyi

Protein namesi
Recommended name:
N5-carboxyaminoimidazole ribonucleotide mutaseUniRule annotation (EC:5.4.99.18UniRule annotation)
Short name:
N5-CAIR mutaseUniRule annotation
Alternative name(s):
5-(carboxyamino)imidazole ribonucleotide mutaseUniRule annotation
Gene namesi
Name:purEUniRule annotationImported
OrganismiAcetobacter acetiImported
Taxonomic identifieri435 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

Pathology & Biotechi

Chemistry databases

DrugBankiDB04272 Citric Acid

Structurei

3D structure databases

SMRiQ2QJL3
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2QJL3

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 173AIRCInterPro annotationAdd BLAST152

Sequence similaritiesi

Belongs to the AIR carboxylase family. Class I subfamily.UniRule annotation

Family and domain databases

Gene3Di3.40.50.7700, 1 hit
HAMAPiMF_01929 PurE_classI, 1 hit
InterProiView protein in InterPro
IPR033747 PurE_ClassI
IPR000031 PurE_dom
IPR024694 PurE_prokaryotes
IPR035893 PurE_sf
PfamiView protein in Pfam
PF00731 AIRC, 1 hit
PIRSFiPIRSF001338 AIR_carboxylase, 1 hit
SMARTiView protein in SMART
SM01001 AIRC, 1 hit
SUPFAMiSSF52255 SSF52255, 1 hit
TIGRFAMsiTIGR01162 purE, 1 hit

Sequencei

Sequence statusi: Complete.

Q2QJL3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSETAPLPSA SSALEDKAAS APVVGIIMGS QSDWETMRHA DALLTELEIP
60 70 80 90 100
HETLIVSAHR TPDRLADYAR TAAERGLNVI IAGAGGAAHL PGMCAAWTRL
110 120 130 140 150
PVLGVPVESR ALKGMDSLLS IVQMPGGVPV GTLAIGASGA KNAALLAASI
160 170 180
LALYNPALAA RLETWRALQT ASVPNSPITE DK
Length:182
Mass (Da):18,735
Last modified:January 24, 2006 - v1
Checksum:iBA1F9245440138E8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ059549 Genomic DNA Translation: AAZ04483.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ059549 Genomic DNA Translation: AAZ04483.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U11X-ray1.55A/B1-182[»]
2FW1X-ray2.00A/B1-182[»]
2FW6X-ray1.85A/B1-182[»]
2FW7X-ray1.75A/B1-182[»]
2FW8X-ray1.75A/B1-182[»]
2FW9X-ray1.75A/B1-182[»]
2FWAX-ray1.90A/B1-182[»]
2FWBX-ray2.00A/B1-182[»]
2FWIX-ray1.94A/B1-182[»]
2FWJX-ray1.95A/B1-182[»]
2FWPX-ray1.85A/B1-182[»]
SMRiQ2QJL3
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB04272 Citric Acid

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayi
UPA00074;UER00943

BRENDAi5.4.99.18 33

Miscellaneous databases

EvolutionaryTraceiQ2QJL3

Family and domain databases

Gene3Di3.40.50.7700, 1 hit
HAMAPiMF_01929 PurE_classI, 1 hit
InterProiView protein in InterPro
IPR033747 PurE_ClassI
IPR000031 PurE_dom
IPR024694 PurE_prokaryotes
IPR035893 PurE_sf
PfamiView protein in Pfam
PF00731 AIRC, 1 hit
PIRSFiPIRSF001338 AIR_carboxylase, 1 hit
SMARTiView protein in SMART
SM01001 AIRC, 1 hit
SUPFAMiSSF52255 SSF52255, 1 hit
TIGRFAMsiTIGR01162 purE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiQ2QJL3_ACEAC
AccessioniPrimary (citable) accession number: Q2QJL3
Entry historyiIntegrated into UniProtKB/TrEMBL: January 24, 2006
Last sequence update: January 24, 2006
Last modified: October 10, 2018
This is version 71 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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