(data stored in ACNUC9543 zone)

SWISSPROT: RBSD_YERPA

ID   RBSD_YERPA              Reviewed;         139 AA.
AC   Q1CC43;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=YPA_0010;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta-
CC       furan 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
CC       5-phosphate from beta-D-ribopyranose: step 1/2.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000308; ABG11979.1; -; Genomic_DNA.
DR   RefSeq; WP_002212252.1; NZ_CP009906.1.
DR   SMR; Q1CC43; -.
DR   EnsemblBacteria; ABG11979; ABG11979; YPA_0010.
DR   KEGG; ypa:YPA_0010; -.
DR   HOGENOM; HOG000219040; -.
DR   KO; K06726; -.
DR   OMA; IIRTGEC; -.
DR   UniPathway; UPA00916; UER00888.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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;
DR   PRODOM; Q1CC43.
DR   SWISS-2DPAGE; Q1CC43.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase.
FT   CHAIN         1    139       D-ribose pyranase.
FT                                /FTId=PRO_0000346304.
FT   REGION      128    130       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01661}.
FT   ACT_SITE     20     20       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01661}.
FT   BINDING      28     28       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01661}.
FT   BINDING     106    106       Substrate. {ECO:0000255|HAMAP-
FT                                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
//

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