Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271Substrate
Binding sitei94 – 941Substrate
Binding sitei230 – 2301ATP
Binding sitei258 – 2581Substrate
Metal bindingi297 – 2971Magnesium or manganeseUniRule annotation
Metal bindingi310 – 3101Magnesium or manganeseUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 16611ATPAdd
BLAST
Nucleotide bindingi199 – 2024ATP

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3613615-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetasePRO_0000148024Add
BLAST

Interactioni

Subunit structurei

Homohexamer. Dimer of trimers.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0136.

Structurei

Secondary structure

1
361
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 118Combined sources
Beta strandi20 – 267Combined sources
Helixi29 – 3810Combined sources
Beta strandi43 – 475Combined sources
Turni49 – 513Combined sources
Helixi53 – 575Combined sources
Beta strandi62 – 665Combined sources
Helixi70 – 745Combined sources
Helixi76 – 849Combined sources
Beta strandi87 – 893Combined sources
Helixi93 – 997Combined sources
Helixi101 – 1066Combined sources
Beta strandi112 – 1143Combined sources
Helixi116 – 1205Combined sources
Turni121 – 1233Combined sources
Helixi125 – 13410Combined sources
Beta strandi142 – 1454Combined sources
Helixi146 – 1483Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi166 – 1716Combined sources
Helixi172 – 18413Combined sources
Beta strandi186 – 1883Combined sources
Helixi190 – 1956Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi204 – 21411Combined sources
Turni215 – 2184Combined sources
Beta strandi219 – 23214Combined sources
Helixi233 – 2364Combined sources
Helixi241 – 2455Combined sources
Beta strandi253 – 2608Combined sources
Helixi265 – 2673Combined sources
Helixi268 – 28518Combined sources
Beta strandi292 – 3009Combined sources
Beta strandi306 – 31510Combined sources
Helixi317 – 3226Combined sources
Helixi329 – 3313Combined sources
Helixi339 – 35315Combined sources
Helixi356 – 3583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R7KX-ray2.10A1-361[»]
2R7LX-ray2.10A1-361[»]
2R7MX-ray2.30A1-361[»]
2R7NX-ray2.40A1-361[»]
ProteinModelPortaliQ57600.
SMRiQ57600. Positions 1-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57600.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini116 – 348233ATP-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.
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.
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.

Genome annotation databases

EnsemblBacteriaiAAB98117; AAB98117; MJ_0136.
KEGGimja:MJ_0136.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R7KX-ray2.10A1-361[»]
2R7LX-ray2.10A1-361[»]
2R7MX-ray2.30A1-361[»]
2R7NX-ray2.40A1-361[»]
ProteinModelPortaliQ57600.
SMRiQ57600. Positions 1-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0136.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98117; AAB98117; MJ_0136.
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.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. "A Methanocaldococcus jannaschii archaeal signature gene encodes for a 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase: a new enzyme in purine biosynthesis."
    Ownby K., Xu H., White R.H.
    J. Biol. Chem. 280:10881-10887(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  3. "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 (2.1 ANGSTROMS) IN COMPLEXES WITH ATP AND SUBSTRATE, SUBUNIT.

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 11, 2015
This is version 94 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.