RBSD_THEMA
ID RBSD_THEMA Reviewed; 135 AA.
AC Q9X054;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=TM_0959;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36038.1; -; Genomic_DNA.
DR PIR; D72311; D72311.
DR RefSeq; NP_228767.1; NC_000853.1.
DR RefSeq; WP_004080603.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X054; -.
DR SMR; Q9X054; -.
DR STRING; 243274.THEMA_09550; -.
DR EnsemblBacteria; AAD36038; AAD36038; TM_0959.
DR KEGG; tma:TM0959; -.
DR eggNOG; COG1869; Bacteria.
DR InParanoid; Q9X054; -.
DR OMA; IIRTGEC; -.
DR OrthoDB; 1750843at2; -.
DR UniPathway; UPA00916; UER00888.
DR Proteomes; UP000008183; 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:0042806; F:fucose binding; IBA:GO_Central.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IBA:GO_Central.
DR GO; GO:0019303; P:D-ribose catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006004; P:fucose metabolic process; IBA:GO_Central.
DR GO; GO:0036065; P:fucosylation; 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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..135
FT /note="D-ribose pyranase"
FT /id="PRO_0000346291"
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 102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 124..126
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ SEQUENCE 135 AA; 14974 MW; 5D2359CED5BAAC8C CRC64;
MKKVGILNSE ISKIVADMGH MDTLAVVDLG FPIPQGVKKV DLVVDRGKPG LMEVIEILLR
ELKVERIILA KEMDEKSIQT KQELLKLIEK MNGPVEVVTV PHKEFKEMSK NVKGIIRTGA
DIPYSNVILV GGVIF
