RBSD_PSEU2
ID RBSD_PSEU2 Reviewed; 134 AA.
AC Q4ZUH3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Psyr_2156;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY37199.1; -; Genomic_DNA.
DR RefSeq; WP_011267465.1; NC_007005.1.
DR RefSeq; YP_235237.1; NC_007005.1.
DR AlphaFoldDB; Q4ZUH3; -.
DR SMR; Q4ZUH3; -.
DR STRING; 205918.Psyr_2156; -.
DR EnsemblBacteria; AAY37199; AAY37199; Psyr_2156.
DR KEGG; psb:Psyr_2156; -.
DR PATRIC; fig|205918.7.peg.2206; -.
DR eggNOG; COG1869; Bacteria.
DR HOGENOM; CLU_135498_0_0_6; -.
DR OMA; IIRTGEC; -.
DR UniPathway; UPA00916; UER00888.
DR Proteomes; UP000000426; 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.
FT CHAIN 1..134
FT /note="D-ribose pyranase"
FT /id="PRO_0000346242"
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 101
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT BINDING 123..125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ SEQUENCE 134 AA; 14521 MW; 4410E905AE52448B CRC64;
MKKTPLLNIA LSRVIASLGH GDILMIVDAG MPVPAGVELI DLALTRGVPD FISVLDVVLS
EMQVESHVLA NEMAEVKPPA LQVIESLNLE DQLGQQRWIS HEDLKVLSRK AKAIIRTGEC
QPYSNVALVS GVVF
