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Protein

Putative ribose 1,5-bisphosphate isomerase

Gene

MJ0601

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of ribose 1,5-bisphosphate to ribulose 1,5-bisphosphate (RuBP), the CO2 acceptor and substrate for RubisCO.Curated

Catalytic activityi

Alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate.

Cofactori

NAD+1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi34 – 6229NADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ribose 1,5-bisphosphate isomerase (EC:5.3.1.29)
Alternative name(s):
Ribulose 1,5-bisphosphate synthase
Short name:
RuBP synthase
Gene namesi
Ordered Locus Names:MJ0601
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 – 267267Putative ribose 1,5-bisphosphate isomerasePRO_0000153947Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi243232.MJ_0601.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 3419Combined sources
Beta strandi36 – 427Combined sources
Helixi46 – 5712Combined sources
Beta strandi62 – 709Combined sources
Turni74 – 785Combined sources
Beta strandi82 – 887Combined sources
Turni89 – 924Combined sources
Helixi93 – 964Combined sources
Turni97 – 993Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi109 – 1135Combined sources
Helixi116 – 12712Combined sources
Beta strandi131 – 14414Combined sources
Beta strandi147 – 1559Combined sources
Helixi156 – 1616Combined sources
Beta strandi168 – 17710Combined sources
Helixi180 – 1823Combined sources
Helixi184 – 1929Combined sources
Helixi207 – 21711Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi225 – 2273Combined sources
Helixi230 – 2356Combined sources
Helixi246 – 26318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y4MX-ray2.71A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ58018.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the THI4 family.Curated

Phylogenomic databases

eggNOGiarCOG00574. Archaea.
COG1635. LUCA.
InParanoidiQ58018.
KOiK03146.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00304. Thi4.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR002922. Thi4_fam.
IPR022828. Thi4_putative.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00292. TIGR00292. 1 hit.

Sequencei

Sequence statusi: Complete.

Q58018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNLMNIKDI KLNADETKTT KAILKASFDM WLDIVEADVV IVGAGPSGLT
60 70 80 90 100
CARYLAKEGF KVVVLERHLA FGGGTWGGGM GFPYIVVEEP ADELLREVGI
110 120 130 140 150
KLIDMGDGYY VADSVEVPAK LAVAAMDAGA KILTGIVVED LILREDGVAG
160 170 180 190 200
VVINSYAIER AGLHIDPLTI RSKVVVDATG HEASIVNILV KKNKLEADVP
210 220 230 240 250
GEKSMWAEKG ENALLRNTRE VYPNLFVCGM AANASHGGYR MGAIFGGMYL
260
SGKLCAELIT EKLKNKE
Length:267
Mass (Da):28,655
Last modified:November 2, 2010 - v3
Checksum:i2F359B900C838251
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98592.1.
PIRiA64375.

Genome annotation databases

EnsemblBacteriaiAAB98592; AAB98592; MJ_0601.
KEGGimja:MJ_0601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98592.1.
PIRiA64375.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4Y4MX-ray2.71A/B/C/D/E/F/G/H1-267[»]
ProteinModelPortaliQ58018.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0601.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98592; AAB98592; MJ_0601.
KEGGimja:MJ_0601.

Phylogenomic databases

eggNOGiarCOG00574. Archaea.
COG1635. LUCA.
InParanoidiQ58018.
KOiK03146.

Family and domain databases

Gene3Di3.50.50.60. 1 hit.
HAMAPiMF_00304. Thi4.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR002922. Thi4_fam.
IPR022828. Thi4_putative.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
TIGRFAMsiTIGR00292. TIGR00292. 1 hit.
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. "Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea."
    Finn M.W., Tabita F.R.
    J. Bacteriol. 186:6360-6366(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION IN CO(2) FIXATION WITH RUBISCO, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiRUBPS_METJA
AccessioniPrimary (citable) accession number: Q58018
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 2, 2010
Last modified: June 8, 2016
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The D-ribose 1,5-bisphosphate used in the reaction appears to originate from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP), which is converted to D-ribose 1,5-bisphosphate nonenzymatically at elevated temperatures in the presence of magnesium in a time-dependent fashion.
M.jannaschii was shown to possess RubisCO activity but no phosphoribulokinase (PRK) activity (PubMed:12730164). Thus, the work done in PubMed:15375115 provided evidence for a previously uncharacterized pathway for RuBP synthesis, and so identified a novel means to synthesize the CO2 acceptor and substrate for RubisCO in the absence of a detectable kinase, such as PRK.

Caution

This protein is proposed to have ribose 1,5-bisphosphate isomerase activity but the recombinant protein does not seem to be active in vitro (PubMed:15375115). In contrast, another protein from M.jannaschii likely possesses this activity (MJ0122).1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  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.