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Protein

5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase

Gene

purP

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP- and formate-dependent formylation of 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates.UniRule annotation

Catalytic activityi

ATP + formate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase (purP)
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-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10Substrate1
Binding sitei11Substrate1
Binding sitei71Substrate1
Binding sitei75Substrate1
Binding sitei204ATP1
Binding sitei232Substrate1
Metal bindingi270Magnesium or manganeseUniRule annotation1
Metal bindingi283Magnesium or manganeseUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi132 – 142ATPAdd BLAST11
Nucleotide bindingi173 – 176ATP4

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00074; UER00134.

Names & Taxonomyi

Protein namesi
Recommended name:
5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetaseUniRule annotation (EC:6.3.4.23UniRule annotation)
Alternative name(s):
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligaseUniRule annotation
Gene namesi
Name:purPUniRule annotation
Ordered Locus Names:PF1517
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003486361 – 3345-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetaseAdd BLAST334

Proteomic databases

PRIDEiQ8U0R7.

Interactioni

Subunit structurei

Homotrimer and homohexamer.1 Publication

Protein-protein interaction databases

STRINGi186497.PF1517.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Helixi13 – 22Combined sources10
Beta strandi27 – 31Combined sources5
Helixi33 – 35Combined sources3
Helixi36 – 40Combined sources5
Beta strandi47 – 50Combined sources4
Helixi56 – 61Combined sources6
Beta strandi64 – 66Combined sources3
Helixi72 – 76Combined sources5
Helixi78 – 82Combined sources5
Beta strandi88 – 90Combined sources3
Helixi94 – 99Combined sources6
Helixi101 – 110Combined sources10
Beta strandi118 – 121Combined sources4
Helixi122 – 124Combined sources3
Beta strandi129 – 133Combined sources5
Turni138 – 141Combined sources4
Beta strandi143 – 147Combined sources5
Helixi148 – 159Combined sources12
Helixi164 – 166Combined sources3
Beta strandi169 – 174Combined sources6
Beta strandi179 – 188Combined sources10
Turni189 – 192Combined sources4
Beta strandi193 – 206Combined sources14
Helixi207 – 212Combined sources6
Helixi215 – 218Combined sources4
Beta strandi227 – 234Combined sources8
Helixi239 – 241Combined sources3
Helixi242 – 259Combined sources18
Beta strandi265 – 273Combined sources9
Beta strandi279 – 285Combined sources7
Helixi290 – 295Combined sources6
Helixi302 – 304Combined sources3
Helixi312 – 325Combined sources14
Helixi329 – 332Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R84X-ray1.90A/B1-334[»]
2R85X-ray1.70A/B1-334[»]
2R86X-ray2.50A/B1-334[»]
2R87X-ray2.30A/B/C/D/E/F1-334[»]
ProteinModelPortaliQ8U0R7.
SMRiQ8U0R7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U0R7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini78 – 325ATP-graspUniRule annotationAdd BLAST248

Sequence similaritiesi

Belongs to the phosphohexose mutase family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04346. Archaea.
COG1759. LUCA.
HOGENOMiHOG000228474.
KOiK06863.
OMAiKGGRGYF.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPiMF_01163. IMP_biosynth_PurP. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR023656. IMP_biosynth_PurP.
IPR009720. IMP_biosynth_PurP_C.
IPR010672. IMP_biosynth_PurP_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF06849. DUF1246. 1 hit.
PF06973. DUF1297. 1 hit.
[Graphical view]
PIRSFiPIRSF004602. ATPgrasp_PurP. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8U0R7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVRIATYAS HSALQILKGA KDEGFETIAF GSSKVKPLYT KYFPVADYFI
60 70 80 90 100
EEKYPEEELL NLNAVVVPTG SFVAHLGIEL VENMKVPYFG NKRVLRWESD
110 120 130 140 150
RNLERKWLKK AGIRVPEVYE DPDDIEKPVI VKPHGAKGGK GYFLAKDPED
160 170 180 190 200
FWRKAEKFLG IKRKEDLKNI QIQEYVLGVP VYPHYFYSKV REELELMSID
210 220 230 240 250
RRYESNVDAI GRIPAKDQLE FDMDITYTVI GNIPIVLRES LLMDVIEAGE
260 270 280 290 300
RVVKAAEELM GGLWGPFCLE GVFTPDLEFV VFEISARIVA GTNIFVNGSP
310 320 330
YTWLRYDRPV STGRRIAMEI REAIENDMLE KVLT
Length:334
Mass (Da):38,298
Last modified:June 1, 2002 - v1
Checksum:i78802D9AB5184900
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81641.1.
RefSeqiWP_011012664.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81641; AAL81641; PF1517.
GeneIDi1469393.
KEGGipfu:PF1517.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81641.1.
RefSeqiWP_011012664.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R84X-ray1.90A/B1-334[»]
2R85X-ray1.70A/B1-334[»]
2R86X-ray2.50A/B1-334[»]
2R87X-ray2.30A/B/C/D/E/F1-334[»]
ProteinModelPortaliQ8U0R7.
SMRiQ8U0R7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1517.

Proteomic databases

PRIDEiQ8U0R7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81641; AAL81641; PF1517.
GeneIDi1469393.
KEGGipfu:PF1517.

Phylogenomic databases

eggNOGiarCOG04346. Archaea.
COG1759. LUCA.
HOGENOMiHOG000228474.
KOiK06863.
OMAiKGGRGYF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00134.

Miscellaneous databases

EvolutionaryTraceiQ8U0R7.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
HAMAPiMF_01163. IMP_biosynth_PurP. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR023656. IMP_biosynth_PurP.
IPR009720. IMP_biosynth_PurP_C.
IPR010672. IMP_biosynth_PurP_N.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF06849. DUF1246. 1 hit.
PF06973. DUF1297. 1 hit.
[Graphical view]
PIRSFiPIRSF004602. ATPgrasp_PurP. 1 hit.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPURP_PYRFU
AccessioniPrimary (citable) accession number: Q8U0R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: June 1, 2002
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.