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   13-SEP-2023, entry version 89.
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; Pseudomonadota; 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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR004379; UDP-GALP_mutase.
DR   InterPro; IPR015899; UDP-GalPyranose_mutase_C.
DR   NCBIfam; TIGR00031; UDP-GALP_mutase; 1.
DR   PANTHER; PTHR21197; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   PANTHER; PTHR21197:SF0; UDP-GALACTOPYRANOSE MUTASE; 1.
DR   Pfam; PF03275; GLF; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 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
//