(data stored in ACNUC7421 zone)

SWISSPROT: RBSD_HISS2

ID   RBSD_HISS2              Reviewed;         139 AA.
AC   B0UV47;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 66.
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=HSM_0089;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000947; ACA32567.1; -; Genomic_DNA.
DR   RefSeq; WP_012341700.1; NC_010519.1.
DR   SMR; B0UV47; -.
DR   EnsemblBacteria; ACA32567; ACA32567; HSM_0089.
DR   GeneID; 31486365; -.
DR   KEGG; hsm:HSM_0089; -.
DR   HOGENOM; HOG000219040; -.
DR   KO; K06726; -.
DR   OMA; IIRTGEC; -.
DR   OrthoDB; 1750843at2; -.
DR   BioCyc; HSOM228400:G1GB8-91-MONOMER; -.
DR   UniPathway; UPA00916; UER00888.
DR   Proteomes; UP000008543; 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; B0UV47.
DR   SWISS-2DPAGE; B0UV47.
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..139
FT                   /note="D-ribose pyranase"
FT                   /id="PRO_0000346212"
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;  15282 MW;  4FCFB82333D5E4B9 CRC64;
     MKKTKLLNAS LSHYIATLGH TDSLVICDAG LPISNQVERV DLALEAGVPG FLQTVDVVIS
     EMFVEHAVVA KEIREKNPQI HDALLDSLRK LSEQQGNCIA VEYVEHEEFK VLSSESKAAV
     RTGEFSPYAN IILYSGVPF
//

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