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Protein

Putative ribose 1,5-bisphosphate isomerase

Gene

MA_2851

Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
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+By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi27 – 5529NADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMACE188937:GI2O-2887-MONOMER.

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:MA_2851
OrganismiMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifieri188937 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000002487 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 260260Putative ribose 1,5-bisphosphate isomerasePRO_0000153946Add
BLAST

Interactioni

Subunit structurei

Homohexamer.By similarity

Protein-protein interaction databases

STRINGi188937.MA2851.

Structurei

3D structure databases

ProteinModelPortaliQ8TM19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the THI4 family.Curated

Phylogenomic databases

eggNOGiarCOG00574. Archaea.
COG1635. LUCA.
InParanoidiQ8TM19.
KOiK03146.
OMAiRMGPVFG.
PhylomeDBiQ8TM19.

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.

Q8TM19-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELDEVIITR AIFDEYSKTF LDYTDIDVAL VGGGPANLVA AKYLAEAGVK
60 70 80 90 100
VALYEQKLSL GGGMWAGGMM FPRIVVQEEA TRILDDFGIR YKEYESGYYV
110 120 130 140 150
ANSVESVGKL IAGATSAGAE VFNLVSFEDI MIRENDRVTG IVINWGPVTT
160 170 180 190 200
QRLHVDPLMI RTKLVIDGTG HEAVVCNTIL RKIPNAKIGE LGLLGEKPMW
210 220 230 240 250
SEVGERLAVN ATQEIYPGLI VAGMAANAAT RAPRMGPVFG GMLLSGEKAA
260
KLALDRLKTI
Length:260
Mass (Da):28,097
Last modified:June 1, 2002 - v1
Checksum:i8C2B378141F9E0C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06230.1.
RefSeqiWP_011022803.1. NC_003552.1.

Genome annotation databases

EnsemblBacteriaiAAM06230; AAM06230; MA_2851.
GeneIDi1474748.
KEGGimac:MA_2851.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE010299 Genomic DNA. Translation: AAM06230.1.
RefSeqiWP_011022803.1. NC_003552.1.

3D structure databases

ProteinModelPortaliQ8TM19.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi188937.MA2851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM06230; AAM06230; MA_2851.
GeneIDi1474748.
KEGGimac:MA_2851.

Phylogenomic databases

eggNOGiarCOG00574. Archaea.
COG1635. LUCA.
InParanoidiQ8TM19.
KOiK03146.
OMAiRMGPVFG.
PhylomeDBiQ8TM19.

Enzyme and pathway databases

BioCyciMACE188937:GI2O-2887-MONOMER.

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. "The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity."
    Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.
    , McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.
    Genome Res. 12:532-542(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35395 / DSM 2834 / JCM 12185 / C2A.
  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: FUNCTION IN CO(2) FIXATION WITH RUBISCO.

Entry informationi

Entry nameiRUBPS_METAC
AccessioniPrimary (citable) accession number: Q8TM19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 1, 2002
Last modified: June 8, 2016
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

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.acetivorans 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 some recombinant ortholog proteins are not active in vitro (PubMed:15375115 and PubMed:17303759). Moreover, another protein from M.acetivorans likely possesses this activity (MA_0379).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.