(data stored in ACNUC7421 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   08-MAY-2019, entry version 25.
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.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73064.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73064.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73064.1,
RC   ECO:0000313|Proteomes:UP000002034};
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.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., 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-
CC       furan 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
CC       5-phosphate from beta-D-ribopyranose: step 1/2.
CC       {ECO:0000256|HAMAP-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   Proteomes; UP000002034; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01661,
KW   ECO:0000256|SAAS:SAAS00421456};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01661,
KW   ECO:0000256|SAAS:SAAS00421475}.
FT   REGION      120    122       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01661}.
FT   COILED       52     72       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE     20     20       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01661}.
FT   BINDING      28     28       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01661}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                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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