RBSD_HAEIN
ID RBSD_HAEIN Reviewed; 139 AA.
AC P44734;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D-ribose pyranase;
DE EC=5.4.99.62;
GN Name=rbsD; OrderedLocusNames=HI_0501;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan
CC forms of D-ribose. {ECO:0000250}.
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;
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 1/2.
CC -!- SUBUNIT: Homodecamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC22159.1; -; Genomic_DNA.
DR PIR; G64072; G64072.
DR RefSeq; NP_438659.1; NC_000907.1.
DR RefSeq; WP_005693672.1; NC_000907.1.
DR AlphaFoldDB; P44734; -.
DR SMR; P44734; -.
DR STRING; 71421.HI_0501; -.
DR DNASU; 949497; -.
DR EnsemblBacteria; AAC22159; AAC22159; HI_0501.
DR KEGG; hin:HI_0501; -.
DR PATRIC; fig|71421.8.peg.520; -.
DR eggNOG; COG1869; Bacteria.
DR HOGENOM; CLU_135498_0_0_6; -.
DR OMA; IIRTGEC; -.
DR PhylomeDB; P44734; -.
DR BioCyc; HINF71421:G1GJ1-514-MON; -.
DR UniPathway; UPA00916; UER00888.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0016866; F:intramolecular transferase activity; IBA:GO_Central.
DR GO; GO:0048029; F:monosaccharide binding; IEA:InterPro.
DR GO; GO:0019303; P:D-ribose catabolic process; IBA:GO_Central.
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_0000097193"
FT ACT_SITE 20
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128..130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15339 MW; C5E424FDDF7A2C67 CRC64;
MKKTALLNAQ LSHCIATLGH TESLTICDAG LPIPLSVERI DLALTAGVPS FLQTLNVVTN
EMYVERVVIA EEIKEKNPEI LTALLTQLQK LESHQGNQIQ VEFVSHETFK KFTLESKAIV
RTGECSPYAN VILYSGVPF
