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Database: UniProt
Entry: A0A178EZH9_TRIRU
LinkDB: A0A178EZH9_TRIRU
Original site: A0A178EZH9_TRIRU 
ID   A0A178EZH9_TRIRU        Unreviewed;       374 AA.
AC   A0A178EZH9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|RuleBase:RU366046};
DE            EC=5.1.3.2 {ECO:0000256|RuleBase:RU366046};
GN   ORFNames=A7C99_4051 {ECO:0000313|EMBL:OAL64617.1};
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL64617.1, ECO:0000313|Proteomes:UP000243015};
RN   [1] {ECO:0000313|EMBL:OAL64617.1, ECO:0000313|Proteomes:UP000243015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA   Zhan P., Tao Y., Liu W.;
RT   "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL   Submitted (MAY-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAL64617.1}.
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DR   EMBL; LHPM01000015; OAL64617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178EZH9; -.
DR   VEuPathDB; FungiDB:TERG_05002; -.
DR   OMA; GEHLICN; -.
DR   OrthoDB; 5489993at2759; -.
DR   UniPathway; UPA00214; -.
DR   Proteomes; UP000243015; 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:UP000243015}.
FT   DOMAIN          6..283
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
FT   REGION          354..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  40844 MW;  63965D65532068BA CRC64;
     MAAGSVLVTG GTGYIGSFTA LALLEAGYKV VVVDSLYNSS EEALNRIELI CGKRPEFVNL
     DVRDEAAFDK VFDAHPDIDS VIHFAALKAV GESTERPLDY YDVNVHGSIC LLRSMVRHNV
     TNIVFSSSAT VYGDATRFPN MIPIPEECPL GPTNPYGNTK VAIESAITDM VNSERARAKR
     AGKPEDVKKW NGALLRYFNP AGAHPSGIMG EDPQGVPYNL LPLLAQVANG KREKLSVFGN
     DYASHDGTAI RDYIHILDLA DGHLEALNYL RANHPGVRAW NLGTGKGSTV LEMVKAFSAA
     VGRDLPYEIA PRRDGDVLDL TSNPSRANKE LGWVAKRDLH QACEDLWRWT ENNPQGYRQS
     PPAALLEKLK AKST
//
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