GALE_BIFL2
ID GALE_BIFL2 Reviewed; 340 AA.
AC E8MF10; A7BJ83;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=UDP-glucose 4-epimerase;
DE EC=5.1.3.2;
DE AltName: Full=UDP-galactose 4-epimerase;
GN Name=lnpD; OrderedLocusNames=BLLJ_1620;
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=17720833; DOI=10.1128/aem.01425-07;
RA Nishimoto M., Kitaoka M.;
RT "Identification of N-acetylhexosamine 1-kinase in the complete lacto-N-
RT biose I/galacto-N-biose metabolic pathway in Bifidobacterium longum.";
RL Appl. Environ. Microbiol. 73:6444-6449(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the
CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through
CC a mechanism involving the transient reduction of NAD. Can also
CC epimerize UDP-GalNAc to UDP-GlcNAc. Involved in the lacto-N-biose
CC I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for
CC host intestinal colonization by bifidobacteria.
CC {ECO:0000269|PubMed:17720833}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose = UDP-alpha-D-galactose;
CC Xref=Rhea:RHEA:22168, ChEBI:CHEBI:58885, ChEBI:CHEBI:66914;
CC EC=5.1.3.2; Evidence={ECO:0000269|PubMed:17720833};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000269|PubMed:17720833}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AB303839; BAF73927.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ67287.1; -; Genomic_DNA.
DR RefSeq; WP_007052336.1; NC_015067.1.
DR PDB; 6K0G; X-ray; 1.80 A; A=1-340.
DR PDB; 6K0H; X-ray; 2.00 A; A=1-340.
DR PDB; 6K0I; X-ray; 1.80 A; A=1-340.
DR PDBsum; 6K0G; -.
DR PDBsum; 6K0H; -.
DR PDBsum; 6K0I; -.
DR AlphaFoldDB; E8MF10; -.
DR SMR; E8MF10; -.
DR GeneID; 66505871; -.
DR KEGG; blm:BLLJ_1620; -.
DR HOGENOM; CLU_007383_1_10_11; -.
DR OMA; NLGNEDW; -.
DR UniPathway; UPA00214; -.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01179; galE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Galactose metabolism; Isomerase;
KW NAD.
FT CHAIN 1..340
FT /note="UDP-glucose 4-epimerase"
FT /id="PRO_0000424073"
FT ACT_SITE 150
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 32..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 59..60
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 81..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 292..295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:6K0G"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 94..114
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6K0I"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 201..209
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 269..280
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6K0G"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:6K0G"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:6K0G"
SQ SEQUENCE 340 AA; 37226 MW; C9DF104EA3ECC690 CRC64;
MTTVLVTGGA GFIATHTDIE LLNKGYDVIS VDNYGNSSPV ALERVEQITG KPVKRYDGDV
RDEALMERVF AENNIDWVIH FAGLKAVGES VAKPIEYYDN NLYSTLVLLK VMKKHNVKKI
IFSSSATVYG TPKELPITEE TPTGGTTNPY GTSKLFQEQI LRDVHVADPS WTIVLLRYFN
PVGAHESGLL GEDPKGIPAN LTPYVAKVAV GELKEVQVYG DDYDTPDGTG VRDYIHVVDL
AKGHVAVIDH IDKEGVFVYN LGTGHGYSVL EVIKAYEKAA GHPIPYAIKP RRPGDIAACY
ADASKAEKEL GWKAELTIDD MAASSLNWQT KNPNGFRDAE
