RBSD_BACSU
ID RBSD_BACSU Reviewed; 131 AA.
AC P36946;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=D-ribose pyranase;
DE EC=5.4.99.62;
GN Name=rbsD; OrderedLocusNames=BSU35930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7921236; DOI=10.1099/13500872-140-8-1829;
RA Woodson K., Devine K.M.;
RT "Analysis of a ribose transport operon from Bacillus subtilis.";
RL Microbiology 140:1829-1838(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH D-RIBOSE AND
RP RIBOSE-5-PHOSPHATE, SUBUNIT, MUTAGENESIS OF HIS-98, AND REACTION MECHANISM.
RX PubMed=12738765; DOI=10.1074/jbc.m304523200;
RA Kim M.-S., Shin J., Lee W., Lee H.-S., Oh B.-H.;
RT "Crystal structures of RbsD leading to the identification of cytoplasmic
RT sugar-binding proteins with a novel folding architecture.";
RL J. Biol. Chem. 278:28173-28180(2003).
CC -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan
CC forms of D-ribose. {ECO:0000250}.
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;
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 1/2.
CC -!- SUBUNIT: Homodecamer; dimer of pentamers.
CC {ECO:0000269|PubMed:12738765}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought (PubMed:7921236 and PubMed:9353933) to
CC be a high affinity ribose transport protein. {ECO:0000305}.
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DR EMBL; Z25798; CAA81050.1; -; Genomic_DNA.
DR EMBL; Z92953; CAB07464.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15610.1; -; Genomic_DNA.
DR PIR; I40464; I40464.
DR RefSeq; NP_391474.1; NC_000964.3.
DR RefSeq; WP_003244175.1; NZ_JNCM01000034.1.
DR PDB; 1OGC; X-ray; 2.00 A; A/B/C/D/E=1-131.
DR PDB; 1OGD; X-ray; 1.95 A; A/B/C/D/E=1-131.
DR PDB; 1OGE; X-ray; 2.05 A; A/B/C/D/E=1-131.
DR PDB; 1OGF; X-ray; 2.30 A; A/B/C/D/E=1-131.
DR PDBsum; 1OGC; -.
DR PDBsum; 1OGD; -.
DR PDBsum; 1OGE; -.
DR PDBsum; 1OGF; -.
DR AlphaFoldDB; P36946; -.
DR SMR; P36946; -.
DR STRING; 224308.BSU35930; -.
DR DrugBank; DB04286; beta-D-Ribopyranose.
DR DrugBank; DB04352; beta-D-Ribose-5-phosphate.
DR jPOST; P36946; -.
DR PaxDb; P36946; -.
DR PRIDE; P36946; -.
DR EnsemblBacteria; CAB15610; CAB15610; BSU_35930.
DR GeneID; 936846; -.
DR KEGG; bsu:BSU35930; -.
DR PATRIC; fig|224308.179.peg.3890; -.
DR eggNOG; COG1869; Bacteria.
DR InParanoid; P36946; -.
DR OMA; IIRTGEC; -.
DR PhylomeDB; P36946; -.
DR BioCyc; BSUB:BSU35930-MON; -.
DR BRENDA; 5.4.99.62; 658.
DR UniPathway; UPA00916; UER00888.
DR EvolutionaryTrace; P36946; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0016866; F:intramolecular transferase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IEA:InterPro.
DR GO; GO:0019303; P:D-ribose catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW Reference proteome.
FT CHAIN 1..131
FT /note="D-ribose pyranase"
FT /id="PRO_0000097190"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 28
FT /ligand="substrate"
FT BINDING 98
FT /ligand="substrate"
FT BINDING 120..122
FT /ligand="substrate"
FT MUTAGEN 98
FT /note="H->A: Reduced sugar-binding affinity."
FT /evidence="ECO:0000269|PubMed:12738765"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1OGD"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1OGD"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1OGD"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1OGD"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1OGD"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1OGD"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:1OGD"
SQ SEQUENCE 131 AA; 14227 MW; 053F1AC529CC98D1 CRC64;
MKKHGILNSH LAKILADLGH TDKIVIADAG LPVPDGVLKI DLSLKPGLPA FQDTAAVLAE
EMAVEKVIAA AEIKASNQEN AKFLENLFSE QEIEYLSHEE FKLLTKDAKA VIRTGEFTPY
ANCILQAGVL F
