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Database: UniProt
Entry: A0A1I0LYY6_9BACT
LinkDB: A0A1I0LYY6_9BACT
Original site: A0A1I0LYY6_9BACT 
ID   A0A1I0LYY6_9BACT        Unreviewed;       146 AA.
AC   A0A1I0LYY6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Ribose 5-phosphate isomerase B {ECO:0000313|EMBL:SEV81013.1};
GN   ORFNames=SAMN04487850_0111 {ECO:0000313|EMBL:SEV81013.1};
OS   Prevotella aff. ruminicola Tc2-24.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=81582 {ECO:0000313|EMBL:SEV81013.1, ECO:0000313|Proteomes:UP000199373};
RN   [1] {ECO:0000313|EMBL:SEV81013.1, ECO:0000313|Proteomes:UP000199373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC2-24 {ECO:0000313|EMBL:SEV81013.1,
RC   ECO:0000313|Proteomes:UP000199373};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family.
CC       {ECO:0000256|ARBA:ARBA00008754}.
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DR   EMBL; FOIQ01000001; SEV81013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0LYY6; -.
DR   Proteomes; UP000199373; Unassembled WGS sequence.
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; IPR004785; RpiB.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   NCBIfam; TIGR01120; rpiB; 1.
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; 1.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:SEV81013.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199373}.
FT   ACT_SITE        68
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT   ACT_SITE        101
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT   BINDING         11..12
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         69..73
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         102
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         112
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         139
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ   SEQUENCE   146 AA;  16289 MW;  D1D90308F7662435 CRC64;
     MEIKTVGVAC DHAGFALKKF VLQYLEEKGY PYKDYGTWSD ASVDYPDFGH ALAEGIESGE
     VYPGIAICGS GEGISITLNK HQQVRAGLCW IPEIAHLIRQ HNDANVLVMP GRFIDNNMAR
     KIMDEFFTAT FEGGRHQKRV DKIAIK
//
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