ID   UGDH_RAT                Reviewed;         493 AA.
AC   O70199;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=UDP-glucose 6-dehydrogenase;
DE            Short=UDP-Glc dehydrogenase;
DE            Short=UDP-GlcDH;
DE            Short=UDPGDH;
DE            EC=1.1.1.22;
GN   Name=Ugdh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Liver;
RA   Kobayashi T., Yokota H., Yuasa A.;
RT   "cDNA cloning of rat UDP-glucose dehydrogenase.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16396499; DOI=10.1021/pr0503073;
RA   Moser K., White F.M.;
RT   "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT   MS/MS.";
RL   J. Proteome Res. 5:98-104(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-474, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Kidney;
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC   -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans;
CC       hyaluronan, chondroitin sulfate, and heparan sulfate.
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP-
CC       glucuronate + 2 NADH.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronic acid
CC       biosynthesis; UDP-glucuronic acid from UDP-glucose: step 1/1.
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; AB013732; BAA28215.1; -; mRNA.
DR   IPI; IPI00195803; -.
DR   RefSeq; NP_112615.1; -.
DR   UniGene; Rn.3967; -.
DR   PhosphoSite; O70199; -.
DR   PRIDE; O70199; -.
DR   Ensembl; ENSRNOG00000002643; Rattus norvegicus.
DR   GeneID; 83472; -.
DR   KEGG; rno:83472; -.
DR   RGD; 621879; Ugdh.
DR   HOVERGEN; O70199; -.
DR   BRENDA; 1.1.1.22; 248.
DR   NextBio; 615885; -.
DR   ArrayExpress; O70199; -.
DR   GermOnline; ENSRNOG00000002643; Rattus norvegicus.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IDA:RGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017476; Nucleotide_sugar_DH.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR014028; UDP-Glc/GDP-Man_DH_dimer-bd.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.1870; UDP-Glc/GDP-Man_DH_C; 1.
DR   PANTHER; PTHR11374; UDPG_MGDP_DH_Creg; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    493       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074062.
FT   NP_BIND       6     23       NAD (By similarity).
FT   REGION      162    165       Substrate binding (By similarity).
FT   ACT_SITE    276    276       Nucleophile (By similarity).
FT   BINDING      36     36       NAD (By similarity).
FT   BINDING      41     41       NAD (By similarity).
FT   BINDING      93     93       NAD (By similarity).
FT   BINDING     131    131       NAD; via amide nitrogen (By similarity).
FT   BINDING     165    165       NAD (By similarity).
FT   BINDING     220    220       Substrate (By similarity).
FT   BINDING     273    273       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     279    279       NAD (By similarity).
FT   BINDING     339    339       Substrate (By similarity).
FT   BINDING     346    346       NAD (By similarity).
FT   MOD_RES     473    473       Phosphotyrosine (By similarity).
FT   MOD_RES     474    474       Phosphothreonine.
SQ   SEQUENCE   493 AA;  54892 MW;  F435D1F9AC8307EF CRC64;
     MVEIKKICCI GAGYVGGPTC SVIARMCPEI RVTVVDVNEA RINAWNSPTL PIYEPGLKEV
     VESCRGKNLF FSTNIDDAIR EADLVFISVN TPTKTYGMGK GRAADLKYIE ACARRIVQNS
     NGYKIVTEKS TVPVRAAESI RRIFDANTKP NLNLQVLSNP EFLAEGTAIK DLKNPDRVLI
     GGDETPEGQR AVQALCAVYE HWVPKEKILT TNTWSSELSK LAANAFLAQR ISSINSISAL
     CESTGADVEE VATAIGMDQR IGNKFLKASV GFGGGCFQKD VLNLVYLCEA LNLPEVARYW
     QQVIDMNDYQ RRRFASRIID SLFNTVTDKK IAILGFAFKK DTGDTRESSS IYISKYLMDE
     GAHLHIYDPK VPREQIVVDL SHPGVSADDQ VSRLVTISKD PYEACDGAHA LVICTEWDMF
     KELDYERIHK RMLKPAFIFD GRRVLDGLHN ELQTIGFQIE TIGKKVSSKR IPYTPGEIPK
     FSLQDPPNKK PKV
//