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Database: UniProt
Entry: A0A0V0VS56_9BILA
LinkDB: A0A0V0VS56_9BILA
Original site: A0A0V0VS56_9BILA 
ID   A0A0V0VS56_9BILA        Unreviewed;       793 AA.
AC   A0A0V0VS56;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=UDP-N-acetylglucosamine 4-epimerase {ECO:0000256|ARBA:ARBA00031827};
DE            EC=5.1.3.2 {ECO:0000256|ARBA:ARBA00013189};
DE            EC=5.1.3.7 {ECO:0000256|ARBA:ARBA00013175};
DE   AltName: Full=UDP-galactose 4-epimerase {ECO:0000256|ARBA:ARBA00031367};
GN   ORFNames=T09_10201 {ECO:0000313|EMBL:KRX66330.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX66330.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX66330.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX66330.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-
CC         galactosamine; Xref=Rhea:RHEA:20517, ChEBI:CHEBI:57705,
CC         ChEBI:CHEBI:67138; EC=5.1.3.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00000014};
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   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Carbohydrate metabolism; galactose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004947}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC
CC       1.A.6) family. {ECO:0000256|ARBA:ARBA00007193,
CC       ECO:0000256|RuleBase:RU000679}.
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:KRX66330.1}.
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DR   EMBL; JYDN01000011; KRX66330.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VS56; -.
DR   STRING; 181606.A0A0V0VS56; -.
DR   Proteomes; UP000054681; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:InterPro.
DR   GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-KW.
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; IPR001873; ENaC.
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; PF00858; ASC; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   PRINTS; PR01713; NUCEPIMERASE.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023144};
KW   Galactose metabolism {ECO:0000256|ARBA:ARBA00023144};
KW   Ion channel {ECO:0000256|RuleBase:RU000679};
KW   Ion transport {ECO:0000256|RuleBase:RU000679};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW   ECO:0000256|RuleBase:RU000679};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW   ECO:0000256|RuleBase:RU000679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000679};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000679}.
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          441..711
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   793 AA;  90001 MW;  0F9769621705F3CB CRC64;
     MGSVNTWYSS LSLTERLLWA AVFFIATGFI LYCWTAIDWT FSDNGPGTTI LHVKKQSMHF
     PPLLLCTRQP FNSKYIRQDP IFNNRFDKYA EKLISFSSAV KIQDLAGNEI EKLEKLYSTS
     FNKTQERETE VNCFLPGDHF LKCIQIIKNV TSGAEILDVS SFCQNSSTLI TGFLNPCTVI
     FPSEQKIPSD LGALKIELEL QKEQLTVSPA EFSGFEIYVG DLTVEAPFLP KITLKNNQAA
     SLKLEIIEYI SSVSSKDFEE NRQALFKIET LKNCLYQSIK DECNCVLPFI CTKPDDSISI
     PLCTVNDYKN CTASLGTNTL EIINHFDQFQ MPCLMKESTV NDIQFNCIAT RLPDIDTQTL
     RYRATFSIYY DHFDYFQIKE AQLDSIKIFI LYGIPLAVVT ALLLITLKYN MVKRVGKRPY
     SDDYLETSET SMYIMPTRKS ILVTGAGGFI GSHVVLELLE NNYNVIAIDT FDNCVRGERY
     PVSLERVMEL TGKRFRFYDA DVLSKETLLE IFKQHRIDSV MHFAGLKAVG ESISKPLEYY
     WTNVGGALTL LRAMKEEHIN NLIFSSSATV YGPPKQLPIN EEQEIGCGLT NPYGRSKFFI
     EQILEDFHAA NTYAFEKEWN IISLRYFNPV GAHPSGLIGE DPTSMPNNLM PNISKAAAGK
     IPALRIFGND YDTVDGTGVR DYIHVVDLAK GHVAALQKLH ENAGYKVYNL GNGKGYSVLQ
     LVEQFERSCG RKIPYVIENR RPGDLAEIYC DNTLARNELN WTPKYDLQQM CVDTWNWQQK
     NPDGYVSSEM ESE
//
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