ID B5YD30_DICT6 Unreviewed; 433 AA.
AC B5YD30;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN OrderedLocusNames=DICTH_0556 {ECO:0000313|EMBL:ACI18567.1};
OS Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12).
OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae;
OC Dictyoglomus.
OX NCBI_TaxID=309799 {ECO:0000313|EMBL:ACI18567.1, ECO:0000313|Proteomes:UP000001733};
RN [1] {ECO:0000313|EMBL:ACI18567.1, ECO:0000313|Proteomes:UP000001733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35947 / DSM 3960 / H-6-12
RC {ECO:0000313|Proteomes:UP000001733};
RX PubMed=24558247;
RA Coil D.A., Badger J.H., Forberger H.C., Riggs F., Madupu R., Fedorova N.,
RA Ward N., Robb F.T., Eisen J.A.;
RT "Complete Genome Sequence of the Extreme Thermophile Dictyoglomus
RT thermophilum H-6-12.";
RL Genome Announc. 2:e00109-e00114(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-
CC alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00000874,
CC ECO:0000256|PIRNR:PIRNR000124};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004701}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601, ECO:0000256|PIRNR:PIRNR000124}.
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DR EMBL; CP001146; ACI18567.1; -; Genomic_DNA.
DR RefSeq; WP_012547199.1; NC_011297.1.
DR AlphaFoldDB; B5YD30; -.
DR STRING; 309799.DICTH_0556; -.
DR PaxDb; 309799-DICTH_0556; -.
DR KEGG; dth:DICTH_0556; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_1_2_0; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000001733; Chromosome.
DR GO; GO:0051287; F:NAD binding; 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 GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR028357; UDPglc_DH_bac.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 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; PIRSF500134; UDPglc_DH_bac; 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, ECO:0000256|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124}.
FT DOMAIN 316..417
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 154..157
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 157
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 206
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 251..255
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 265
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 330
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
SQ SEQUENCE 433 AA; 48855 MW; CB9139179D1367AF CRC64;
MRKIGIVGTG YIGLVTGLGL ADFGNKVTCF DVDYEKIEKL KNGISPIKEK NIDELLKRNI
ENKRITFTTN IQELLENSEI IFVCVNTPPK EDGNVDLSQI ISVSENLAQN IKDKKIIAIK
STVPIGTLEK ITLIFEKYGK RKDQDFELAV VPEFLREGNA VYDFFNPSRI VIGAENPETI
EKLKEVFLPL NAPIVVTSPN AAILIKYASN AFLAMRISFI NEIANIAEKF GIDIKEVIEG
MKYDKRIGKD YLQPGIGFGG PCLGKDLMGL IKMAEKEGYH PSLLISIFEK NEHQIRQIIY
KIKFFLGEFL DNQTIGILGL TFKPDTNDVR NSLALRIIKM LKNDGAKIKA YDPLGIDEAK
KEIQDIEYYD NPYDVAKDSN CLVILTGWKE FKELDFRKIK DVMKTPIIID GVNLLDPKTI
KEMGFIYKGV GRQ
//
