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Protein

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

Gene

purP

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 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 annotation1 Publication

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+1 Publication, Mn2+1 PublicationNote: Binds 1 Mg2+ or Mn2+ ion per subunit.1 Publication

Enzyme regulationi

Inhibited by ADP.1 Publication

pH dependencei

Optimum pH is 6.25.1 Publication

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 sitei27Substrate1
Binding sitei94Substrate1
Binding sitei230ATP1
Binding sitei258Substrate1
Metal bindingi297Magnesium or manganeseUniRule annotation1
Metal bindingi310Magnesium or manganeseUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi156 – 166ATPAdd BLAST11
Nucleotide bindingi199 – 202ATP4

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

BioCyciMetaCyc:MONOMER-14616.
BRENDAi6.3.4.23. 3260.
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:MJ0136
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480241 – 3615-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetaseAdd BLAST361

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0136.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 11Combined sources8
Beta strandi20 – 26Combined sources7
Helixi29 – 38Combined sources10
Beta strandi43 – 47Combined sources5
Turni49 – 51Combined sources3
Helixi53 – 57Combined sources5
Beta strandi62 – 66Combined sources5
Helixi70 – 74Combined sources5
Helixi76 – 84Combined sources9
Beta strandi87 – 89Combined sources3
Helixi93 – 99Combined sources7
Helixi101 – 106Combined sources6
Beta strandi112 – 114Combined sources3
Helixi116 – 120Combined sources5
Turni121 – 123Combined sources3
Helixi125 – 134Combined sources10
Beta strandi142 – 145Combined sources4
Helixi146 – 148Combined sources3
Beta strandi153 – 156Combined sources4
Beta strandi166 – 171Combined sources6
Helixi172 – 184Combined sources13
Beta strandi186 – 188Combined sources3
Helixi190 – 195Combined sources6
Beta strandi197 – 200Combined sources4
Beta strandi204 – 214Combined sources11
Turni215 – 218Combined sources4
Beta strandi219 – 232Combined sources14
Helixi233 – 236Combined sources4
Helixi241 – 245Combined sources5
Beta strandi253 – 260Combined sources8
Helixi265 – 267Combined sources3
Helixi268 – 285Combined sources18
Beta strandi292 – 300Combined sources9
Beta strandi306 – 315Combined sources10
Helixi317 – 322Combined sources6
Helixi329 – 331Combined sources3
Helixi339 – 353Combined sources15
Helixi356 – 358Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R7KX-ray2.10A1-361[»]
2R7LX-ray2.10A1-361[»]
2R7MX-ray2.30A1-361[»]
2R7NX-ray2.40A1-361[»]
ProteinModelPortaliQ57600.
SMRiQ57600.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57600.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini116 – 348ATP-graspUniRule annotationAdd BLAST233

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG04346. Archaea.
COG1759. LUCA.
InParanoidiQ57600.
KOiK06863.
OMAiCIHYFYS.
PhylomeDBiQ57600.

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.

Q57600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISKDEILEI FDKYNKDEIT IATLGSHTSL HILKGAKLEG FSTVCITMKG
60 70 80 90 100
RDVPYKRFKV ADKFIYVDNF SDIKNEEIQE KLRELNSIVV PHGSFIAYCG
110 120 130 140 150
LDNVENSFLV PMFGNRRILR WESERSLEGK LLREAGLRVP KKYESPEDID
160 170 180 190 200
GTVIVKFPGA RGGRGYFIAS STEEFYKKAE DLKKRGILTD EDIANAHIEE
210 220 230 240 250
YVVGTNFCIH YFYSPLKDEV ELLGMDKRYE SNIDGLVRIP AKDQLEMNIN
260 270 280 290 300
PSYVITGNIP VVIRESLLPQ VFEMGDKLVA KAKELVPPGM IGPFCLQSLC
310 320 330 340 350
NENLELVVFE MSARVDGGTN SFMNGGPYSF LYNGEPLSMG QRIAREIKMA
360
LQLDMIDKII S
Length:361
Mass (Da):40,824
Last modified:November 1, 1997 - v1
Checksum:i0B9928DDD41D4DB6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98117.1.
PIRiH64316.
RefSeqiWP_010869629.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98117; AAB98117; MJ_0136.
GeneIDi1450977.
KEGGimja:MJ_0136.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98117.1.
PIRiH64316.
RefSeqiWP_010869629.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R7KX-ray2.10A1-361[»]
2R7LX-ray2.10A1-361[»]
2R7MX-ray2.30A1-361[»]
2R7NX-ray2.40A1-361[»]
ProteinModelPortaliQ57600.
SMRiQ57600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98117; AAB98117; MJ_0136.
GeneIDi1450977.
KEGGimja:MJ_0136.

Phylogenomic databases

eggNOGiarCOG04346. Archaea.
COG1759. LUCA.
InParanoidiQ57600.
KOiK06863.
OMAiCIHYFYS.
PhylomeDBiQ57600.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00134.
BioCyciMetaCyc:MONOMER-14616.
BRENDAi6.3.4.23. 3260.

Miscellaneous databases

EvolutionaryTraceiQ57600.

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_METJA
AccessioniPrimary (citable) accession number: Q57600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 96 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.