GLF8_KLEPN
ID GLF8_KLEPN Reviewed; 384 AA.
AC Q48481;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Probable UDP-galactopyranose mutase;
DE Short=UGM;
DE EC=5.4.99.9;
DE AltName: Full=UDP-GALP mutase;
DE AltName: Full=Uridine 5-diphosphate galactopyranose mutase;
DE Flags: Precursor;
GN Name=rfbD;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype O8;
RX PubMed=8752339; DOI=10.1128/jb.178.17.5205-5214.1996;
RA Kelly R.F., Whitfield C.;
RT "Clonally diverse rfb gene clusters are involved in expression of a family
RT of related D-galactan O antigens in Klebsiella species.";
RL J. Bacteriol. 178:5205-5214(1996).
CC -!- FUNCTION: Catalyzes the interconversion through a 2-keto intermediate
CC of uridine diphosphogalactopyranose (UDP-GalP) into uridine
CC diphosphogalactofuranose (UDP-GalF). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-galactose = UDP-alpha-D-galactofuranose;
CC Xref=Rhea:RHEA:24132, ChEBI:CHEBI:66914, ChEBI:CHEBI:66915;
CC EC=5.4.99.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; L41518; AAC98408.1; -; Genomic_DNA.
DR AlphaFoldDB; Q48481; -.
DR SMR; Q48481; -.
DR BindingDB; Q48481; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0008767; F:UDP-galactopyranose mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004379; UDP-GALP_mutase.
DR InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR Pfam; PF03275; GLF; 1.
DR TIGRFAMs; TIGR00031; UDP-GALP_mutase; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Isomerase; Lipopolysaccharide biosynthesis; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..384
FT /note="Probable UDP-galactopyranose mutase"
FT /id="PRO_0000087507"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 33..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 60..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 349
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250"
FT BINDING 350..355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 384 AA; 44475 MW; AA812676E6D060FF CRC64;
MNNKNIMIVG AGFSGVVIAR QLAEQGYTVK IIDRRDHIGG NSYDTRDPQT DVMVHVYGPH
IFHTDNETVW NYVNQYAEMM PYVNRVKATV NGQVFSLPIN LHTINQFFAK TCSPDEARAL
ISEKGDSSIV EPQTFEEQAL RFIGKELYEA FFKGYTIKQW GMEPSELPAS ILKRLPVRFN
YDDNYFNHKF QGMPKLGYTR MIEAIADHEN ISIELQREFL PEEREDYAHV FYSGPLDAFY
SYQYGRLGYR TLDFEKFTYQ GDYQGCAVMN YCSIDVPYTR ITEHKYFSPW ESHEGSVCYK
EYSRACGEND IPYYPIRQMG EMALLEKYLS LAESEKNITF VGRLGTYRYL DMDVTIAEAL
KTADEFLSSV ANQEEMPVFT VPVR
