RBSD_CITK8
ID RBSD_CITK8 Reviewed; 139 AA.
AC A8ACQ4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 69.
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=CKO_00088;
OS Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter.
OX NCBI_TaxID=290338;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG The Citrobacter koseri Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (AUG-2007) 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}.
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DR EMBL; CP000822; ABV11267.1; -; Genomic_DNA.
DR RefSeq; WP_024130088.1; NC_009792.1.
DR AlphaFoldDB; A8ACQ4; -.
DR SMR; A8ACQ4; -.
DR STRING; 290338.CKO_00088; -.
DR EnsemblBacteria; ABV11267; ABV11267; CKO_00088.
DR GeneID; 45134389; -.
DR KEGG; cko:CKO_00088; -.
DR HOGENOM; CLU_135498_1_0_6; -.
DR OrthoDB; 1750843at2; -.
DR UniPathway; UPA00916; UER00888.
DR Proteomes; UP000008148; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0062193; F:D-ribose pyranase activity; IEA:UniProtKB-EC.
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;
KW Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..139
FT /note="D-ribose pyranase"
FT /id="PRO_0000346183"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ SEQUENCE 139 AA; 15223 MW; C85E0361F18FD69F CRC64;
MKKGAVLNSD ISSVISRLGH TDTLVVCDAG LPVPSSTTRI DMALTQGVPS FMQVLDVVTR
EMQVEAAILA TEIKEHNPQL HETLLSHIEQ LQQHQGNTIE IRYTTHEHFK KLTADSQAVI
RSGECSPYAN VILCAGVTF
