ID A0A1L9VCX4_ASPGL Unreviewed; 373 AA.
AC A0A1L9VCX4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|RuleBase:RU366046};
DE EC=5.1.3.2 {ECO:0000256|RuleBase:RU366046};
GN ORFNames=ASPGLDRAFT_176905 {ECO:0000313|EMBL:OJJ81733.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ81733.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878905; OJJ81733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9VCX4; -.
DR STRING; 1160497.A0A1L9VCX4; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_176905; -.
DR OrthoDB; 5489993at2759; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000184300; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184300}.
FT DOMAIN 6..285
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 373 AA; 40569 MW; 66128AE1BD86E4BD CRC64;
MSAGSVLVTG GTGYIGSFTT LALVEAGYKV VVADNLYNSS DEALKRVELI SGKKPEFAQL
DVTDEAAFDK VFEAHPDIDS VIHFAALKAV GESGEKPLDY YHVNVFGTLC LLRSMIRHDV
TNIVFSSSAT VYGDATRFPD MIPIPENCPL GPTNPYGNTK FAVETAITDL INAQRNNALK
AGNQAEAQKW NGALLRYFNP AGSHPSGIMG EDPQGVPYNL LPLLAQVATG KREKLLVFGD
AIDYESRDGT AIRDYIHILD LANGHLKALN YLRANNPGVR AWNLGTGKGS TVYEMINAFS
AAVGRDLAYE VAPRRAGDVL NLTANPTRAH SELGWTAERT LEQACEDLWL WTRNNPQGYR
QEPPAELLAA LKK
//
