ID   RBSD_BACC4              Reviewed;         131 AA.
AC   B7HBU7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=D-ribose pyranase {ECO:0000255|HAMAP-Rule:MF_01661};
DE            EC=5.4.99.62 {ECO:0000255|HAMAP-Rule:MF_01661};
GN   Name=rbsD {ECO:0000255|HAMAP-Rule:MF_01661};
GN   OrderedLocusNames=BCB4264_A0698;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan
CC       forms of D-ribose. {ECO:0000255|HAMAP-Rule:MF_01661}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-ribopyranose = beta-D-ribofuranose;
CC         Xref=Rhea:RHEA:25432, ChEBI:CHEBI:27476, ChEBI:CHEBI:47002;
CC         EC=5.4.99.62; Evidence={ECO:0000255|HAMAP-Rule:MF_01661};
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_01661}.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01661}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01661}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01661}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001176; ACK59148.1; -; Genomic_DNA.
DR   RefSeq; WP_000716136.1; NZ_VEHB01000008.1.
DR   AlphaFoldDB; B7HBU7; -.
DR   SMR; B7HBU7; -.
DR   EnsemblBacteria; ACK59148; ACK59148; BCB4264_A0698.
DR   KEGG; bcb:BCB4264_A0698; -.
DR   HOGENOM; CLU_135498_0_0_9; -.
DR   OMA; IIRTGEC; -.
DR   UniPathway; UPA00916; UER00888.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0062193; F:D-ribose pyranase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048029; F:monosaccharide binding; IEA:InterPro.
DR   GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1650.10; -; 1.
DR   HAMAP; MF_01661; D_rib_pyranase; 1.
DR   InterPro; IPR023064; D-ribose_pyranase.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR007721; RbsD_FucU.
DR   PANTHER; PTHR37831; PTHR37831; 1.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; SSF102546; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase.
FT   CHAIN           1..131
FT                   /note="D-ribose pyranase"
FT                   /id="PRO_1000187133"
FT   ACT_SITE        20
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         120..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ   SEQUENCE   131 AA;  14211 MW;  1F63540E4A63F8CA CRC64;
     MKKHGVLNSE IAAVLASLGH TDTIVIADCG LPIPDGVKRI DLAVEIGKPS FLDVLQVVAD
     DMAIEKVTLA EEVIINNAEV NKEIEQKLIE PAFEYVSHEQ FKAHTKKAKA IIRTGEATPY
     ANVILHAGVI F