ID F6X1R3_CIOIN Unreviewed; 362 AA.
AC F6X1R3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=UDP-glucose 4-epimerase {ECO:0000256|RuleBase:RU366046};
DE EC=5.1.3.2 {ECO:0000256|RuleBase:RU366046};
GN Name=LOC100182970 {ECO:0000313|Ensembl:ENSCINP00000017186.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000017186.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000017186.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes two distinct but analogous reactions: the
CC reversible epimerization of UDP-glucose to UDP-galactose and the
CC reversible epimerization of UDP-N-acetylglucosamine to UDP-N-
CC acetylgalactosamine. The reaction with UDP-Gal plays a critical role in
CC the Leloir pathway of galactose catabolism in which galactose is
CC converted to the glycolytic intermediate glucose 6-phosphate. It
CC contributes to the catabolism of dietary galactose and enables the
CC endogenous biosynthesis of both UDP-Gal and UDP-GalNAc when exogenous
CC sources are limited. Both UDP-sugar interconversions are important in
CC the synthesis of glycoproteins and glycolipids.
CC {ECO:0000256|ARBA:ARBA00002760}.
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 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 -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366046}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000256|ARBA:ARBA00007637, ECO:0000256|RuleBase:RU366046}.
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DR EMBL; EAAA01000780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6X1R3; -.
DR STRING; 7719.ENSCINP00000017186; -.
DR Ensembl; ENSCINT00000017186.3; ENSCINP00000017186.3; ENSCING00000008426.3.
DR GeneTree; ENSGT00940000158000; -.
DR HOGENOM; CLU_007383_1_10_1; -.
DR InParanoid; F6X1R3; -.
DR OMA; ATDNIGC; -.
DR TreeFam; TF105800; -.
DR UniPathway; UPA00214; -.
DR Proteomes; UP000008144; Chromosome 11.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IBA:GO_Central.
DR GO; GO:0003974; F:UDP-N-acetylglucosamine 4-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0033499; P:galactose catabolic process via UDP-galactose; IBA:GO_Central.
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; IPR016040; NAD(P)-bd_dom.
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; PF16363; GDP_Man_Dehyd; 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|RuleBase:RU366046};
KW Isomerase {ECO:0000256|RuleBase:RU366046};
KW NAD {ECO:0000256|RuleBase:RU366046};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 9..346
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 362 AA; 40755 MW; ECD743285F75E7DE CRC64;
MNVCRKTILV AGGAGYIGSH TVVELLNAGY RVVVIDNLSN AQQNPEDDDD LPPSLVRAKK
ITGKECLHFV KENICDIEKL NVVFDTYNID AVFDFSGRKA VGESTVLPML YYKYNINGTM
NLLKCMRQHE VRDFLFSSSC TVYGAPDQES LPIKEEDSSG CCHCPYAKCK YFIECLLDDL
AKGEPDYWRI MVMRYFNPVG AHESGLMGED PKGDPLNLLP KLAQVATGKR AILDVYGEDY
DTKDGSPIRD YVHVMDVAEA HVKAVKHFQE KYVSTSGIEI YNIGSGRGKS TWEMVKAFEA
ACGKPIQFRV CQRRPGDVPA IYCDPSKAER QLGWKAERSL QEMCEDLWRF YVLNPNGYEE
SN
//
