ID C5D949_GEOSW Unreviewed; 426 AA.
AC C5D949;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:ACS25902.1};
GN OrderedLocusNames=GWCH70_3259 {ECO:0000313|EMBL:ACS25902.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25902.1};
RN [1] {ECO:0000313|EMBL:ACS25902.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS25902.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP001638; ACS25902.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D949; -.
DR STRING; 471223.GWCH70_3259; -.
DR KEGG; gwc:GWCH70_3259; -.
DR eggNOG; COG0677; Bacteria.
DR HOGENOM; CLU_023810_3_1_9; -.
DR OrthoDB; 9803238at2; -.
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 CDD; cd02440; AdoMet_MTases; 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: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}.
FT DOMAIN 313..414
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 426 AA; 46910 MW; 3D7B37A8EF8F5D2B CRC64;
MNRKIAVVGL GYVGLPVAVA FGKKGRIIGF DINEHRINTL KQGIDYTKEV ESQDLLEADI
DFTNDPSRLR EADFIIVAVP TPITETKQPD LTPLIKASET VGSNLQKGAI VVYESTVYPG
ATEEVCVPVL EKASGLKAGV DFFVGYSPER INPGDKEHTF TKITKVVSGQ NDEVLEIIAG
VYGSVVEAGV YRASSIKVAE AAKVIENTQR DLNIALMNEL AIIFDKLGID TAEVLEAAGT
KWNFLPFTPG LVGGHCIGVD PYYLTHKAES VGYHPEVILA GRRINDNMGK FIATSLVKQM
IHQNMPIQGA RVTVLGLTFK ENVPDLRNSK VIDVIRELQE FGVEVQVTDA LADKDEAVRE
YGIELVDYDK LIPADAVVLA VPHDEYVEKG WEQFDRLLKH GKGIVVDIKS KLEKETCPKQ
IKLWRL
//
