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Database: UniProt
Entry: K2D019_9BACT
LinkDB: K2D019_9BACT
Original site: K2D019_9BACT 
ID   K2D019_9BACT            Unreviewed;       174 AA.
AC   K2D019;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ribose-5-phosphate isomerase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_30C00005G0025 {ECO:0000313|EMBL:EKD91457.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD91457.1};
RN   [1] {ECO:0000313|EMBL:EKD91457.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC       {ECO:0000256|ARBA:ARBA00008754}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD91457.1}.
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DR   EMBL; AMFJ01011904; EKD91457.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2D019; -.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   NCBIfam; TIGR00689; rpiB_lacA_lacB; 1.
DR   PANTHER; PTHR30345:SF0; DNA DAMAGE-REPAIR_TOLERATION PROTEIN DRT102; 1.
DR   PANTHER; PTHR30345; RIBOSE-5-PHOSPHATE ISOMERASE B; 1.
DR   Pfam; PF02502; LacAB_rpiB; 2.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 2.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 2.
PE   3: Inferred from homology;
FT   BINDING         14..15
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         74..78
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         125
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         135
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         159
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         163
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ   SEQUENCE   174 AA;  19329 MW;  03EA0BBACE0AA29E CRC64;
     MHYKFSMKIY IGADHTGFEL KEKIRTYLSE LGHEVEDCGA FEYDKSDDYP DFIAKTAQSV
     SKDLENSLGI VIGGSGQGEA MAANKIKGIR CALFYGPALA VEAIDINGNS SDDPYEILKL
     TRIHNGANVL SLGVRFLTEA QAKEAVKVWL DAPFATEDRH IKRIEKIKKI EEKS
//
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