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Database: UniProt
Entry: Q5NEZ5_FRATT
LinkDB: Q5NEZ5_FRATT
Original site: Q5NEZ5_FRATT 
ID   Q5NEZ5_FRATT            Unreviewed;       436 AA.
AC   Q5NEZ5; A0A0G2RM13;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=UDP-glucose/GDP-mannose dehydrogenase {ECO:0000313|EMBL:CAG46093.1};
DE            EC=1.1.1.- {ECO:0000313|EMBL:CAG46093.1};
GN   Name=wbtE {ECO:0000313|EMBL:CAG46093.1};
GN   OrderedLocusNames=FTT_1460c {ECO:0000313|EMBL:CAG46093.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46093.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG46093.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; AJ749949; CAG46093.1; -; Genomic_DNA.
DR   RefSeq; WP_003022298.1; NZ_CP010290.1.
DR   RefSeq; YP_170397.1; NC_006570.2.
DR   AlphaFoldDB; Q5NEZ5; -.
DR   EnsemblBacteria; CAG46093; CAG46093; FTT_1460c.
DR   KEGG; ftu:FTT_1460c; -.
DR   PATRIC; fig|177416.36.peg.1315; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43491:SF2; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 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   PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CAG46093.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT   DOMAIN          322..424
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   436 AA;  48866 MW;  4FD3FC0FEC71B3D4 CRC64;
     MSLYEDIVAK REKVSLVGLG YVGLPIAIAF AKKIDVLGFD ICETKVQHYK DGFDPTKEVG
     DEAVRNTTMK FSCDETSLKE CKFHIVAVPT PVKADKTPDL TPIIKASETV GRNLVKGAYV
     VFESTVYPGV TEDVCVPILE KESGLRSGED FKVGYSPERI NPGDKVHRLE TIIKVVSGMD
     EESLDTIAKV YELVVDAGVY RASSIKVAEA AKVIENSQRD VNIAFVNELS IIFNQMGIDT
     LEVLAAAATK WNFLNFKPGL VGGHCIGVDP YYLTYKAAEL GYHSQVILSG RRINDSMGKF
     VVENLVKKLI SADIPVKRAR VAIFGFTFKE DCPDTRNTRV IDMVKELNEY GIEPYIIDPV
     ADKEEAKHEY GLEFDDLSKM VNLDAIIIAV SHEQFKDITK QQFDRLYAHN SRKIIFDIKG
     SLDKSEFEKD YIYWRL
//
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