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RBSD_OCEIH
ID   RBSD_OCEIH              Reviewed;         131 AA.
AC   Q8ENB2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, 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=OB2575;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC14531.1; -; Genomic_DNA.
DR   RefSeq; WP_011066968.1; NC_004193.1.
DR   AlphaFoldDB; Q8ENB2; -.
DR   SMR; Q8ENB2; -.
DR   STRING; 221109.22778261; -.
DR   EnsemblBacteria; BAC14531; BAC14531; BAC14531.
DR   KEGG; oih:OB2575; -.
DR   eggNOG; COG1869; Bacteria.
DR   HOGENOM; CLU_135498_0_0_9; -.
DR   OMA; IIRTGEC; -.
DR   OrthoDB; 1750843at2; -.
DR   PhylomeDB; Q8ENB2; -.
DR   UniPathway; UPA00916; UER00888.
DR   Proteomes; UP000000822; 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..131
FT                   /note="D-ribose pyranase"
FT                   /id="PRO_0000346226"
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         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
FT   BINDING         120..122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01661"
SQ   SEQUENCE   131 AA;  14273 MW;  EB38EC9CCB71726B CRC64;
     MKKKGMLNSE ISKVLSDLGH TDQIVIADAG LPVPEGVTKI DVALTPGTPS FLDVLKAVKA
     DMVIEGVTLA REIKVDNTEN HKQIQEVIND IPITYVTHEQ FKALSKQAKA IIRTGEITPY
     ANCILQSGVF F
 
 
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