(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BI13_GEOS0

ID   A0A0F6BI13_GEOS0        Unreviewed;       132 AA.
AC   A0A0F6BI13;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 29.
DE   RecName: Full=D-ribose pyranase {ECO:0000256|HAMAP-Rule:MF_01661, ECO:0000256|SAAS:SAAS00015077};
DE            EC=5.4.99.62 {ECO:0000256|HAMAP-Rule:MF_01661, ECO:0000256|SAAS:SAAS00342828};
GN   Name=rbsD {ECO:0000256|HAMAP-Rule:MF_01661};
GN   OrderedLocusNames=GY4MC1_0215 {ECO:0000313|EMBL:ADP73064.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73064.1};
RN   [1] {ECO:0000313|EMBL:ADP73064.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73064.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan
CC       forms of D-ribose. {ECO:0000256|HAMAP-Rule:MF_01661,
CC       ECO:0000256|SAAS:SAAS00342831}.
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:0000256|HAMAP-Rule:MF_01661,
CC         ECO:0000256|SAAS:SAAS01117947};
CC   -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC       phosphate from beta-D-ribopyranose: step 1/2. {ECO:0000256|HAMAP-
CC       Rule:MF_01661, ECO:0000256|SAAS:SAAS00011494}.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000256|HAMAP-Rule:MF_01661,
CC       ECO:0000256|SAAS:SAAS00342803}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01661,
CC       ECO:0000256|SAAS:SAAS00015081}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01661, ECO:0000256|SAAS:SAAS00539081}.
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DR   EMBL; CP002293; ADP73064.1; -; Genomic_DNA.
DR   RefSeq; WP_013399870.1; NC_014650.1.
DR   EnsemblBacteria; ADP73064; ADP73064; GY4MC1_0215.
DR   KEGG; gmc:GY4MC1_0215; -.
DR   KO; K06726; -.
DR   OMA; IIRTGEC; -.
DR   OrthoDB; 1750843at2; -.
DR   BioCyc; GSP581103:G1GOQ-257-MONOMER; -.
DR   UniPathway; UPA00916; UER00888.
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; A0A0F6BI13.
DR   SWISS-2DPAGE; A0A0F6BI13.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01661,
KW   ECO:0000256|SAAS:SAAS00421463}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01661, ECO:0000256|SAAS:SAAS00421456};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01661, ECO:0000256|SAAS:SAAS00421475}.
FT   REGION          120..122
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01661"
FT   COILED          52..72
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        20
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01661"
FT   BINDING         28
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01661"
FT   BINDING         98
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01661"
SQ   SEQUENCE   132 AA;  14605 MW;  B44B64BF21BA62CF CRC64;
     MKKRGILNKD LSMLLASLGH TDTIVIADCG LPIPNGTDRI DLSLVKGFPP FLSVLDAVLE
     ELEVEALTLA EEIKKENPIM YENIQQRLSD VPMQFVPHEQ LKEMTKSAKA VIRTGEATPY
     ANIILRSGVN FS
//

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