ID   UDG_RICPR               Reviewed;         434 AA.
AC   O05973;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-NOV-2008, entry version 54.
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=udg; OrderedLocusNames=RP779;
OS   Rickettsia prowazekii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=782;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   MEDLINE=97419517; PubMed=9274032;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genomic rearrangements during evolution of the obligate intracellular
RT   parasite Rickettsia prowazekii as inferred from an analysis of 52015
RT   bp nucleotide sequence.";
RL   Microbiology 143:2783-2795(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   MEDLINE=99039499; PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O.,
RA   Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K.,
RA   Eriksson A.-S., Winkler H.H., Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- CATALYTIC ACTIVITY: UDP-glucose + 2 NAD(+) + H(2)O = UDP-
CC       glucuronate + 2 NADH.
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-glucuronate
CC       biosynthesis; UDP-glucuronate from UDP-glucose: step 1/1.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family.
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DR   EMBL; Y11785; CAA72478.1; -; Genomic_DNA.
DR   EMBL; AJ235273; CAA15205.1; -; Genomic_DNA.
DR   PIR; E71638; E71638.
DR   RefSeq; NP_221129.1; -.
DR   HSSP; P11759; 1MFZ.
DR   GeneID; 883765; -.
DR   GenomeReviews; AJ235269_GR; RP779.
DR   KEGG; rpr:RP779; -.
DR   HOGENOM; O05973; -.
DR   BioCyc; RPRO272947:RP779-MON; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013328; DHase_multihelical.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR017476; Nucleotide_sugar_DH.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DHase_C.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DHase_dimer.
DR   InterPro; IPR014028; UDP-Glc/GDP-Man_DHase_dimer-bd.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DHase_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 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.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase.
FT   CHAIN         1    434       UDP-glucose 6-dehydrogenase.
FT                                /FTId=PRO_0000074052.
FT   NP_BIND       2     19       NAD (Potential).
FT   ACT_SITE    260    260       By similarity.
SQ   SEQUENCE   434 AA;  48226 MW;  15991BA7112D5036 CRC64;
     MNITFIGSGY VGLVSGIIMG YLGHNVTCLD NDDVKISKLN KKILPIYEAK LDEYLKHALE
     SDRLKFTNIY SNEFRNFDAI FITVGTPSKE LGEADLKYVY DAVDKVSKHI NKDCLIVIKS
     TVPPGSCNNI IAYLKAKGFS FNVASNPEFL REGSAVEDFL YPDRIVVGVN NKESEALLRK
     IYAPLIEQGA KFLVTNLVTS ELIKYVSNSF LATKIAFINE MADLCEKIGA NIKDLSQGVG
     LDQRIGRNFL NAGPGFGGSC FPKDILALNN LVENHKIDCK ILKSVIKSNK LRPSNMVAKI
     ATLLDGDLKG RNIAILGLTY KAGTDDVRAS PAIEIITILL NKDVYVKAFD PIGLENAKKN
     LEHKNLLYFA SAVEACKSVD IIVIATEWSE FKELNWQEIY NLVKSPMIID LRNILDNEVM
     KKIGFRYYAV GSQI
//