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Protein

Ribose-5-phosphate isomerase A

Gene

rpiA

Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.UniRule annotation

Catalytic activityi

D-ribose 5-phosphate = D-ribulose 5-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei109 – 1091Proton acceptorCurated
Binding sitei127 – 1271SubstrateUniRule annotation2 Publications

GO - Molecular functioni

  1. ribose-5-phosphate isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pentose-phosphate shunt, non-oxidative branch Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciFTUL177416:GNBP-1226-MONOMER.
UniPathwayiUPA00115; UER00412.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribose-5-phosphate isomerase AUniRule annotation (EC:5.3.1.6UniRule annotation)
Alternative name(s):
Phosphoriboisomerase AUniRule annotation
Short name:
PRIUniRule annotation
Gene namesi
Name:rpiAUniRule annotation
Ordered Locus Names:FTT_1208
OrganismiFrancisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Taxonomic identifieri177416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
ProteomesiUP000001174 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Ribose-5-phosphate isomerase APRO_0000158419Add
BLAST

Interactioni

Subunit structurei

Homodimer and homotetramer.UniRule annotation2 Publications

Protein-protein interaction databases

STRINGi177416.FTT_1208.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2114Combined sources
Beta strandi26 – 327Combined sources
Helixi36 – 449Combined sources
Helixi45 – 484Combined sources
Turni49 – 513Combined sources
Beta strandi52 – 587Combined sources
Helixi60 – 689Combined sources
Helixi76 – 794Combined sources
Beta strandi81 – 877Combined sources
Beta strandi90 – 923Combined sources
Beta strandi102 – 1043Combined sources
Helixi106 – 1149Combined sources
Beta strandi119 – 1246Combined sources
Helixi125 – 1273Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi137 – 1415Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 15611Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi173 – 1797Combined sources
Helixi185 – 1939Combined sources
Beta strandi198 – 2047Combined sources
Beta strandi210 – 2167Combined sources
Turni217 – 2193Combined sources
Beta strandi220 – 2245Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KWMX-ray2.32A/B/C/D1-224[»]
4IO1X-ray1.65A/B1-224[»]
ProteinModelPortaliQ5NFM5.
SMRiQ5NFM5. Positions 8-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 374Substrate bindingCurated
Regioni87 – 904Substrate bindingUniRule annotation
Regioni100 – 1034Substrate bindingCurated

Sequence similaritiesi

Belongs to the ribose 5-phosphate isomerase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0120.
HOGENOMiHOG000276368.
KOiK01807.
OMAiGACHVQE.
OrthoDBiEOG67MF61.

Family and domain databases

HAMAPiMF_00170. Rib_5P_isom_A.
InterProiIPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5NFM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFFNKKNNQD ELKKLAATEA AKSITTEITL GVGTGSTVGF LIEELVNYRD
60 70 80 90 100
KIKTVVSSSE DSTRKLKALG FDVVDLNYAG EIDLYIDGAD ECNNHKELIK
110 120 130 140 150
GGGAALTREK ICVAAAKKFI CIIDESKKVN TLGNFPLPIE VIPMARSYIA
160 170 180 190 200
RQIVKLGGQP VYREQTITDN GNVILDVYNL KIDNPLKLET ELNQITGVVT
210 220
NGIFALKPAD TVIMATKDSN IVVL
Length:224
Mass (Da):24,466
Last modified:February 1, 2005 - v1
Checksum:i46ACC58D7487CC2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45841.1.
RefSeqiYP_170167.1. NC_006570.2.

Genome annotation databases

EnsemblBacteriaiCAG45841; CAG45841; FTT_1208.
GeneIDi3192024.
KEGGiftu:FTT_1208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ749949 Genomic DNA. Translation: CAG45841.1.
RefSeqiYP_170167.1. NC_006570.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KWMX-ray2.32A/B/C/D1-224[»]
4IO1X-ray1.65A/B1-224[»]
ProteinModelPortaliQ5NFM5.
SMRiQ5NFM5. Positions 8-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi177416.FTT_1208.

Protocols and materials databases

DNASUi3192024.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAG45841; CAG45841; FTT_1208.
GeneIDi3192024.
KEGGiftu:FTT_1208.

Phylogenomic databases

eggNOGiCOG0120.
HOGENOMiHOG000276368.
KOiK01807.
OMAiGACHVQE.
OrthoDBiEOG67MF61.

Enzyme and pathway databases

UniPathwayiUPA00115; UER00412.
BioCyciFTUL177416:GNBP-1226-MONOMER.

Family and domain databases

HAMAPiMF_00170. Rib_5P_isom_A.
InterProiIPR004788. Ribose5P_isomerase_typA.
IPR020672. Ribose5P_isomerase_typA_subgr.
[Graphical view]
PANTHERiPTHR11934. PTHR11934. 1 hit.
PfamiPF06026. Rib_5-P_isom_A. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00021. rpiA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SCHU S4 / Schu 4.
  2. "Crystal structure of ribose-5-isomerase A."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Orlikowska M., Rostankowski R., Nakka C., Hattne J., Grimshaw S., Borek D., Otwinowski Z.
    Submitted (NOV-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.
  3. "Structural and biophysical studies of Ribose-5-Phosphate Isomerase A from Francisella tularensis."
    Center for Structural Genomics of Infectious Diseases (CSGID)
    Rostankowski R., Orlikowska M., Nakka C., Grimshaw S., Borek D., Otwinowski Z.
    Submitted (DEC-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, SUBUNIT.

Entry informationi

Entry nameiRPIA_FRATT
AccessioniPrimary (citable) accession number: Q5NFM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: January 7, 2015
This is version 63 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

External Data

Dasty 3

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 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.