RBSD_YERPY
ID RBSD_YERPY Reviewed; 139 AA.
AC B1JR25;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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}; OrderedLocusNames=YPK_4210;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-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}.
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DR EMBL; CP000950; ACA70466.1; -; Genomic_DNA.
DR RefSeq; WP_002212252.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JR25; -.
DR SMR; B1JR25; -.
DR EnsemblBacteria; ACA70466; ACA70466; YPK_4210.
DR GeneID; 66843601; -.
DR KEGG; ypy:YPK_4210; -.
DR PATRIC; fig|502800.11.peg.560; -.
DR OMA; IIRTGEC; -.
DR UniPathway; UPA00916; UER00888.
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..139
FT /note="D-ribose pyranase"
FT /id="PRO_1000187173"
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 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ SEQUENCE 139 AA; 15234 MW; 4D02B12EC4C3895A CRC64;
MKKGVLLNAD ISAVISRLGH TDQIVIGDAG LPIPATTTRI DLALTRGVPG FLQVVDVVTQ
EMQVENAYLA EEIVKNNPQL HEALLVLLTQ LEQRQENQIA LRYISHEAFK EQTKQSRAVI
RSGECSPFAN IILGSGVTF
