RBSD_ECO81
ID RBSD_ECO81 Reviewed; 139 AA.
AC B7N2I7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=ECED1_4438;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928162; CAR10558.2; -; Genomic_DNA.
DR RefSeq; WP_001314250.1; NC_011745.1.
DR AlphaFoldDB; B7N2I7; -.
DR SMR; B7N2I7; -.
DR EnsemblBacteria; CAR10558; CAR10558; ECED1_4438.
DR KEGG; ecq:ECED1_4438; -.
DR HOGENOM; CLU_135498_0_0_6; -.
DR OMA; IIRTGEC; -.
DR UniPathway; UPA00916; UER00888.
DR Proteomes; UP000000748; 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..139
FT /note="D-ribose pyranase"
FT /id="PRO_1000187145"
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; 15281 MW; 1F58469D64D3F686 CRC64;
MKKGTVLNSD ISSVISRLGH TDTLVVCDAG LPIPKSATRI DMALTQGVPS FMQVLGVVTN
EMQVEAVIIA EEIKQHNPQL HETLLTHLEQ LQQHQGNTIE IRYTTHEQFK QQTAESQAVI
RSGECSPYAN IILCAGVTF
