ID M1QV26_BACTU Unreviewed; 412 AA.
AC M1QV26;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=UDP-glucose dehydrogenase {ECO:0000313|EMBL:AGG04109.1};
DE EC=1.1.1.22 {ECO:0000313|EMBL:AGG04109.1};
GN ORFNames=H175_ch5400 {ECO:0000313|EMBL:AGG04109.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG04109.1, ECO:0000313|Proteomes:UP000011719};
RN [1] {ECO:0000313|EMBL:AGG04109.1, ECO:0000313|Proteomes:UP000011719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGG04109.1};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP004123; AGG04109.1; -; Genomic_DNA.
DR RefSeq; WP_001003088.1; NC_020376.1.
DR AlphaFoldDB; M1QV26; -.
DR SMR; M1QV26; -.
DR GeneID; 67469522; -.
DR KEGG; btht:H175_ch5400; -.
DR PATRIC; fig|1286404.3.peg.5435; -.
DR HOGENOM; CLU_023810_3_2_9; -.
DR Proteomes; UP000011719; 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:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
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:SF1; 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:AGG04109.1}.
FT DOMAIN 316..411
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 412 AA; 45709 MW; 7BB7E18AF5AFC531 CRC64;
MNEKICVVGL GYIGLPTASL LATKGFQVYG VDVNESAVEM INSGKVHIYE PDLDIMVKAA
VQSGNLKAGI VPETSDIFIL AVPTPFKGDH KPDLTYVEQA TKTIAPYIKP GDLVILESTS
PVGTTEKVTE WILEEREDLT VTEEINSNKG VFFVAHCPER VLPGHILREL VENDRIIGGI
NQKSTKKTVD FYKKFVKGKI LETNARTAEM AKLTENSFRD VNIAFANELS IICDELHINV
WELISLANRH PRVNILQPGP GVGGHCIAVD PWFIVDAVPE QAKLIHAARK VNDYKPGYVV
DKIREKADKF KNPIIACLGL AFKANIDDLR ESPSVEIVKY LTDLDVGEVK VVEPHINSLP
KDLVDKDIEL VNLYEAITIA DIIVVLVDHE VFYSIDKNIL KEKIVIDTRG II
//
