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Database: UniProt
Entry: Q3LFG8_PROFR
LinkDB: Q3LFG8_PROFR
Original site: Q3LFG8_PROFR 
ID   Q3LFG8_PROFR            Unreviewed;       148 AA.
AC   Q3LFG8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Ribose-5-phosphate isomerase 1 {ECO:0000313|EMBL:CAD48940.1};
DE            EC=5.3.1.6 {ECO:0000313|EMBL:CAD48940.1};
GN   Name=rpiB1 {ECO:0000313|EMBL:CAD48940.1};
OS   Propionibacterium freudenreichii subsp. shermanii.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Propionibacterium.
OX   NCBI_TaxID=1752 {ECO:0000313|EMBL:CAD48940.1};
RN   [1] {ECO:0000313|EMBL:CAD48940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: CIP103027 {ECO:0000313|EMBL:CAD48940.1};
RA   Meurice G., Dimova D.;
RT   "Metabolic reconstruction of glycolysis pathway in Propionibacterium
RT   shermanii.";
RL   Submitted (SEP-2002) 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; AJ509171; CAD48940.1; -; Genomic_DNA.
DR   RefSeq; WP_013162119.1; NZ_OVTV01000184.1.
DR   AlphaFoldDB; Q3LFG8; -.
DR   OMA; YPPFCLR; -.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
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; PTHR43732:SF1; RIBOSE 5-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR43732; RIBOSE 5-PHOSPHATE ISOMERASE-RELATED; 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:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAD48940.1}.
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT   ACT_SITE        98
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-1"
FT   BINDING         8..9
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         66..70
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         99
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         109
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         132
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
FT   BINDING         136
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005384-2"
SQ   SEQUENCE   148 AA;  15428 MW;  2309C7D3DE776CAE CRC64;
     MRIAMGSDHA GFELKEHLKG YLQGKGHDVI DVGTHSTESV DYPVYGAGAA RKVAAGEADR
     AIVVCGTGLG IGMAAGKVPG IRCAIVSEVY SAQMSRLHND ANALALGARV IGTGVAEEIV
     DVWTTTDFLG GRHGRRVDMI EDPPALDA
//
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