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RBSD_SALTY
ID   RBSD_SALTY              Reviewed;         139 AA.
AC   Q8ZKW0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=STM3881;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL22739.1; -; Genomic_DNA.
DR   RefSeq; NP_462780.1; NC_003197.2.
DR   RefSeq; WP_000715944.1; NC_003197.2.
DR   PDB; 3E7N; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-139.
DR   PDBsum; 3E7N; -.
DR   AlphaFoldDB; Q8ZKW0; -.
DR   SMR; Q8ZKW0; -.
DR   STRING; 99287.STM3881; -.
DR   PaxDb; Q8ZKW0; -.
DR   EnsemblBacteria; AAL22739; AAL22739; STM3881.
DR   GeneID; 1255408; -.
DR   KEGG; stm:STM3881; -.
DR   PATRIC; fig|99287.12.peg.4111; -.
DR   HOGENOM; CLU_135498_0_0_6; -.
DR   OMA; IIRTGEC; -.
DR   PhylomeDB; Q8ZKW0; -.
DR   BioCyc; SENT99287:STM3881-MON; -.
DR   UniPathway; UPA00916; UER00888.
DR   EvolutionaryTrace; Q8ZKW0; -.
DR   Proteomes; UP000001014; 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   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..139
FT                   /note="D-ribose pyranase"
FT                   /id="PRO_0000346253"
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"
FT   STRAND          1..5
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   HELIX           9..17
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          23..27
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   HELIX           73..76
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   HELIX           78..95
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          100..104
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   HELIX           106..113
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:3E7N"
FT   STRAND          131..135
FT                   /evidence="ECO:0007829|PDB:3E7N"
SQ   SEQUENCE   139 AA;  15189 MW;  879C16F6C2A1DE62 CRC64;
     MKKGTVLNSE ISSVISRLGH TDTLVVCDAG LPIPNSTARI DMALTQGVPS FMQVVDVVTR
     EMQVEAAILA TEIKQQNPQL HETLLTHLEQ LQQHQGNTIK ISYTTHEQFK KLTADSQAVI
     RSGECSPYAN VILCAGVTF
 
 
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