(data stored in SCRATCH9089 zone)

SWISSPROT: RBSD_PASMU

ID   RBSD_PASMU              Reviewed;         139 AA.
AC   Q9CP97;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 88.
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=PM0156;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; AE004439; AAK02240.1; -; Genomic_DNA.
DR   RefSeq; WP_005751129.1; NC_002663.1.
DR   SMR; Q9CP97; -.
DR   EnsemblBacteria; AAK02240; AAK02240; PM0156.
DR   KEGG; pmu:PM0156; -.
DR   PATRIC; fig|272843.6.peg.161; -.
DR   eggNOG; ENOG4105MRB; Bacteria.
DR   eggNOG; COG1869; LUCA.
DR   HOGENOM; HOG000219040; -.
DR   KO; K06726; -.
DR   OMA; IIRTGEC; -.
DR   BioCyc; PMUL272843:G1FZ8-164-MONOMER; -.
DR   UniPathway; UPA00916; UER00888.
DR   Proteomes; UP000000809; 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; Q9CP97.
DR   SWISS-2DPAGE; Q9CP97.
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..139
FT                   /note="D-ribose pyranase"
FT                   /id="PRO_0000346228"
FT   REGION          128..130
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   ACT_SITE        20
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         28
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         106
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ   SEQUENCE   139 AA;  15240 MW;  408ABD7717CA0254 CRC64;
     MKKTALLNAP LSQVIATLGH TDSLTICDAG LPIPKQIERV DLALSAGVPS FLQTFHAVVT
     EMFVERAIIA EEIKEKNPKI LTALLNSLAQ LEQQQGNQIE VQYVSHDMFK TYTHASKAIV
     RSGECSPYAN IILYSGVPF
//

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