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FUCM_KLEP3
ID   FUCM_KLEP3              Reviewed;         140 AA.
AC   B5XUY2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=L-fucose mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
DE            EC=5.1.3.29 {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Fucose 1-epimerase {ECO:0000255|HAMAP-Rule:MF_01662};
DE   AltName: Full=Type-2 mutarotase {ECO:0000255|HAMAP-Rule:MF_01662};
GN   Name=fucU {ECO:0000255|HAMAP-Rule:MF_01662}; OrderedLocusNames=KPK_0962;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
CC   -!- FUNCTION: Involved in the anomeric conversion of L-fucose.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-L-fucose = beta-L-fucose; Xref=Rhea:RHEA:25580,
CC         ChEBI:CHEBI:42548, ChEBI:CHEBI:42589; EC=5.1.3.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01662};
CC   -!- PATHWAY: Carbohydrate metabolism; L-fucose metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01662}.
CC   -!- SIMILARITY: Belongs to the RbsD / FucU family. FucU mutarotase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01662}.
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DR   EMBL; CP000964; ACI11510.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XUY2; -.
DR   SMR; B5XUY2; -.
DR   EnsemblBacteria; ACI11510; ACI11510; KPK_0962.
DR   KEGG; kpe:KPK_0962; -.
DR   HOGENOM; CLU_120075_1_0_6; -.
DR   OMA; MGHGDDI; -.
DR   OrthoDB; 1750843at2; -.
DR   UniPathway; UPA00956; -.
DR   Proteomes; UP000001734; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042806; F:fucose binding; IEA:InterPro.
DR   GO; GO:0036373; F:L-fucose mutarotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042354; P:L-fucose metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1650.10; -; 1.
DR   HAMAP; MF_01662; L_fucose_rotase; 1.
DR   InterPro; IPR023751; L-fucose_mutarotase.
DR   InterPro; IPR023750; RbsD-like_sf.
DR   InterPro; IPR007721; RbsD_FucU.
DR   Pfam; PF05025; RbsD_FucU; 1.
DR   SUPFAM; SSF102546; SSF102546; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Fucose metabolism; Isomerase.
FT   CHAIN           1..140
FT                   /note="L-fucose mutarotase"
FT                   /id="PRO_1000187187"
FT   ACT_SITE        22
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
FT   BINDING         129..131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01662"
SQ   SEQUENCE   140 AA;  15322 MW;  B597219A1889489B CRC64;
     MLKTISPLIS PELLKVLAEM GHGDEIIFSD AHFPAHSMGP QVIRADGLRV SDLLQAIIPL
     FELDSYAPPL VMMAAVEGDA LDPTVEQCYR QALSAQAPCP DIVRIDRFAF YDRAQKAFAI
     VITGERAKYG NILLKKGVTP
 
 
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