GLF1_KLEPN
ID GLF1_KLEPN Reviewed; 384 AA.
AC Q48485;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=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=K20 / Serotype O1;
RX PubMed=7559323; DOI=10.1128/jb.177.19.5411-5418.1995;
RA Clarke B.R., Bronner D., Keenleyside W.J., Severn W.B., Richards J.C.,
RA Whitfield C.;
RT "Role of Rfe and RfbF in the initiation of biosynthesis of D-galactan I,
RT the lipopolysaccharide O antigen from Klebsiella pneumoniae serotype O1.";
RL J. Bacteriol. 177:5411-5418(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, COFACTOR, AND SUBUNIT.
RC STRAIN=K20 / Serotype O1;
RX PubMed=9020123; DOI=10.1074/jbc.272.7.4121;
RA Koplin R., Brisson J.R., Whitfield C.;
RT "UDP-galactofuranose precursor required for formation of the
RT lipopolysaccharide O antigen of Klebsiella pneumoniae serotype O1 is
RT synthesized by the product of the rfbDKPO1 gene.";
RL J. Biol. Chem. 272:4121-4128(1997).
RN [3]
RP REACTION MECHANISM.
RC STRAIN=K20 / Serotype O1;
RX PubMed=15133501; DOI=10.1038/nsmb772;
RA Soltero-Higgin M., Carlson E.E., Gruber T.D., Kiessling L.L.;
RT "A unique catalytic mechanism for UDP-galactopyranose mutase.";
RL Nat. Struct. Mol. Biol. 11:539-543(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH FAD, COFACTOR, AND
RP SUBUNIT.
RX PubMed=15843027; DOI=10.1016/j.jmb.2005.02.057;
RA Beis K., Srikannathasan V., Liu H., Fullerton S.W., Bamford V.A.,
RA Sanders D.A., Whitfield C., McNeil M.R., Naismith J.H.;
RT "Crystal structures of Mycobacteria tuberculosis and Klebsiella pneumoniae
RT UDP-galactopyranose mutase in the oxidised state and Klebsiella pneumoniae
RT UDP-galactopyranose mutase in the (active) reduced state.";
RL J. Mol. Biol. 348:971-982(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD AND
RP SUBSTRATE, COFACTOR, AND SUBUNIT.
RX PubMed=19719175; DOI=10.1021/bi901437v;
RA Gruber T.D., Westler W.M., Kiessling L.L., Forest K.T.;
RT "X-ray crystallography reveals a reduced substrate complex of UDP-
RT galactopyranose mutase poised for covalent catalysis by flavin.";
RL Biochemistry 48:9171-9173(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD AND
RP SUBSTRATE, AND COFACTOR.
RX PubMed=19500588; DOI=10.1016/j.jmb.2009.05.081;
RA Gruber T.D., Borrok M.J., Westler W.M., Forest K.T., Kiessling L.L.;
RT "Ligand binding and substrate discrimination by UDP-galactopyranose
RT mutase.";
RL J. Mol. Biol. 391:327-340(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-383 IN COMPLEX WITH FAD,
RP COFACTOR, AND SUBUNIT.
RA Gruber T.D., Dimond M.C., Kiessling L.L., Forest K.T.;
RT "Structure of UDP-galactopyranose mutase bound to flavin mononucleotide.";
RL Submitted (DEC-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of the galactose-containing O-
CC side-chain polysaccharide backbone structure of D-galactan I which is a
CC key component of lipopolysaccharide (LPS). Catalyzes the
CC interconversion through a 2-keto intermediate of uridine
CC diphosphogalactopyranose (UDP-GalP) into uridine
CC diphosphogalactofuranose (UDP-GalF) which is the biosynthetic precursor
CC of galactofuranosyl residues. {ECO:0000269|PubMed:9020123}.
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; Evidence={ECO:0000269|PubMed:9020123};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15843027, ECO:0000269|PubMed:19500588,
CC ECO:0000269|PubMed:19719175, ECO:0000269|PubMed:9020123,
CC ECO:0000269|Ref.7};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:15843027,
CC ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
CC ECO:0000269|PubMed:9020123, ECO:0000269|Ref.7};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15843027,
CC ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
CC ECO:0000269|PubMed:9020123, ECO:0000269|Ref.7}.
CC -!- DISRUPTION PHENOTYPE: Abolishes lipopolysaccharide (LPS) biosynthesis.
CC {ECO:0000269|PubMed:9020123}.
CC -!- SIMILARITY: Belongs to the UDP-galactopyranose/dTDP-fucopyranose mutase
CC family. {ECO:0000305}.
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DR EMBL; L31762; AAC98417.1; -; Genomic_DNA.
DR RefSeq; WP_023284018.1; NZ_WTCT01000132.1.
DR PDB; 1WAM; X-ray; 2.35 A; A=1-384.
DR PDB; 2BI7; X-ray; 2.00 A; A=1-384.
DR PDB; 2BI8; X-ray; 2.35 A; A=1-384.
DR PDB; 3GF4; X-ray; 2.45 A; A/B=1-384.
DR PDB; 3INR; X-ray; 2.30 A; A/B=1-383.
DR PDB; 3INT; X-ray; 2.51 A; A/B=1-384.
DR PDB; 3KYB; X-ray; 2.30 A; A/B=1-384.
DR PDBsum; 1WAM; -.
DR PDBsum; 2BI7; -.
DR PDBsum; 2BI8; -.
DR PDBsum; 3GF4; -.
DR PDBsum; 3INR; -.
DR PDBsum; 3INT; -.
DR PDBsum; 3KYB; -.
DR AlphaFoldDB; Q48485; -.
DR SMR; Q48485; -.
DR BRENDA; 5.4.99.9; 2814.
DR UniPathway; UPA00281; -.
DR EvolutionaryTrace; Q48485; -.
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 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Isomerase;
KW Lipopolysaccharide biosynthesis; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..384
FT /note="UDP-galactopyranose mutase"
FT /id="PRO_0000087506"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 33..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 60..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 84
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 151
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 156
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 160
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 185
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 270
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 280
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 314
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT BINDING 349
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT BINDING 350..355
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15843027,
FT ECO:0000269|PubMed:19500588, ECO:0000269|PubMed:19719175,
FT ECO:0000269|Ref.7"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:2BI7"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2BI7"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:2BI7"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 249..261
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 294..305
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:2BI7"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:2BI7"
FT HELIX 352..371
FT /evidence="ECO:0007829|PDB:2BI7"
SQ SEQUENCE 384 AA; 44457 MW; B74EC65EA5B751AB CRC64;
MKSKKILIVG AGFSGAVIGR QLAEKGHQVH IIDQRDHIGG NSYDARDSET NVMVHVYGPH
IFHTDNETVW NYVNKHAEMM PYVNRVKATV NGQVFSLPIN LHTINQFFSK TCSPDEARAL
IAEKGDSTIA DPQTFEEQAL RFIGKELYEA FFKGYTIKQW GMQPSELPAS ILKRLPVRFN
YDDNYFNHKF QGMPKCGYTQ MIKSILNHEN IKVDLQREFI VEERTHYDHV FYSGPLDAFY
GYQYGRLGYR TLDFKKFTYQ GDYQGCAVMN YCSVDVPYTR ITEHKYFSPW EQHDGSVCYK
EYSRACEEND IPYYPIRQMG EMALLEKYLS LAENETNITF VGRLGTYRYL DMDVTIAEAL
KTAEVYLNSL TENQPMPVFT VSVR
