ID A0A194VHN4_9PEZI Unreviewed; 370 AA.
AC A0A194VHN4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|RuleBase:RU366046};
DE EC=5.1.3.2 {ECO:0000256|RuleBase:RU366046};
GN ORFNames=VM1G_10573 {ECO:0000313|EMBL:KUI63646.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI63646.1};
RN [1] {ECO:0000313|EMBL:KUI63646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI63646.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is
CC active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and
CC lactose. {ECO:0000256|ARBA:ARBA00037676}.
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:0000256|ARBA:ARBA00000083,
CC ECO:0000256|RuleBase:RU366046};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|ARBA:ARBA00001911,
CC ECO:0000256|RuleBase:RU366046};
CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC {ECO:0000256|ARBA:ARBA00004947, ECO:0000256|RuleBase:RU366046}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366046}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|RuleBase:RU366046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the aldose epimerase
CC family. {ECO:0000256|ARBA:ARBA00038238}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NAD(P)-dependent
CC epimerase/dehydratase family. {ECO:0000256|ARBA:ARBA00037955}.
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DR EMBL; KN796114; KUI63646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VHN4; -.
DR OrthoDB; 5489993at2759; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000078559; Unassembled WGS sequence.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05247; UDP_G4E_1_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.90.25.10; UDP-galactose 4-epimerase, domain 1; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005886; UDP_G4E.
DR NCBIfam; TIGR01179; galE; 1.
DR PANTHER; PTHR43725; UDP-GLUCOSE 4-EPIMERASE; 1.
DR PANTHER; PTHR43725:SF51; UDP-GLUCOSE 4-EPIMERASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU366046};
KW Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW Isomerase {ECO:0000256|RuleBase:RU366046};
KW NAD {ECO:0000256|RuleBase:RU366046}.
FT DOMAIN 7..282
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 370 AA; 40984 MW; EF0570EF192321F3 CRC64;
MAPVGTVLVT GGTGYIGSFT SLALLENGYE VVIVDNLYNS SKVALDRIEL ICGKRPKFYE
ADITDKPALD KIFTENPEID SVIHFAALKA VGESGEIPLE YYRVNVGGSI SLMRSMTEHN
VTNIVFSSSA TVYGDATRFP NMIPIPENCP IGPTNTYGRT KSMIENVIED HITAQRNVLK
KAGKPYEQWN GANLRYFNPC GAHPTGIMGE DPQGVPYNLL PLLGQVATGQ REKLLVFGDD
YSSRDGTAIR DYIHVCDLAR GHLVALNYLR KHQPGVKAWN LGSGRGSTVF EMIKAFSKVV
GRDLKYDVVE RRQGDVLDLT ANPGLANKEL NWKTELKMED ACEDLWRWVS NNPQGYRQDP
PAELLEALKK
//
