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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Substrate
Binding sitei11 – 111Substrate
Binding sitei71 – 711Substrate
Binding sitei75 – 751Substrate
Binding sitei204 – 2041ATP
Binding sitei232 – 2321Substrate
Metal bindingi270 – 2701Magnesium or manganeseUniRule annotation
Metal bindingi283 – 2831Magnesium or manganeseUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi132 – 14211ATPAdd
BLAST
Nucleotide bindingi173 – 1764ATP

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3343345-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetasePRO_0000348636Add
BLAST

Proteomic databases

PRIDEiQ8U0R7.

Interactioni

Subunit structurei

Homotrimer and homohexamer.1 Publication

Protein-protein interaction databases

STRINGi186497.PF1517.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi13 – 2210Combined sources
Beta strandi27 – 315Combined sources
Helixi33 – 353Combined sources
Helixi36 – 405Combined sources
Beta strandi47 – 504Combined sources
Helixi56 – 616Combined sources
Beta strandi64 – 663Combined sources
Helixi72 – 765Combined sources
Helixi78 – 825Combined sources
Beta strandi88 – 903Combined sources
Helixi94 – 996Combined sources
Helixi101 – 11010Combined sources
Beta strandi118 – 1214Combined sources
Helixi122 – 1243Combined sources
Beta strandi129 – 1335Combined sources
Turni138 – 1414Combined sources
Beta strandi143 – 1475Combined sources
Helixi148 – 15912Combined sources
Helixi164 – 1663Combined sources
Beta strandi169 – 1746Combined sources
Beta strandi179 – 18810Combined sources
Turni189 – 1924Combined sources
Beta strandi193 – 20614Combined sources
Helixi207 – 2126Combined sources
Helixi215 – 2184Combined sources
Beta strandi227 – 2348Combined sources
Helixi239 – 2413Combined sources
Helixi242 – 25918Combined sources
Beta strandi265 – 2739Combined sources
Beta strandi279 – 2857Combined sources
Helixi290 – 2956Combined sources
Helixi302 – 3043Combined sources
Helixi312 – 32514Combined sources
Helixi329 – 3324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-334.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U0R7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 325248ATP-graspUniRule annotationAdd
BLAST

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.
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
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. Positions 1-334.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii."
    Zhang Y., White R.H., Ealick S.E.
    Biochemistry 47:205-217(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH ATP AND SUBSTRATE, SUBUNIT.

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 11, 2015
This is version 85 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.