ID W0IUB2_9BACT Unreviewed; 458 AA.
AC W0IUB2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=OPIT5_05105 {ECO:0000313|EMBL:AHF89697.1};
OS Opitutaceae bacterium TAV5.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=794903 {ECO:0000313|EMBL:AHF89697.1, ECO:0000313|Proteomes:UP000003813};
RN [1] {ECO:0000313|EMBL:AHF89697.1, ECO:0000313|Proteomes:UP000003813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV5 {ECO:0000313|EMBL:AHF89697.1};
RX PubMed=25744998;
RA Kotak M., Isanapong J., Goodwin L., Bruce D., Chen A., Han C.S.,
RA Huntemann M., Ivanova N., Land M.L., Nolan M., Pati A., Woyke T.,
RA Rodrigues J.L.;
RT "Complete Genome Sequence of the Opitutaceae Bacterium Strain TAV5, a
RT Potential Facultative Methylotroph of the Wood-Feeding Termite
RT Reticulitermes flavipes.";
RL Genome Announc. 3:0-0(2015).
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; CP007053; AHF89697.1; -; Genomic_DNA.
DR AlphaFoldDB; W0IUB2; -.
DR STRING; 794903.OPIT5_05105; -.
DR KEGG; obt:OPIT5_05105; -.
DR eggNOG; COG1004; Bacteria.
DR HOGENOM; CLU_023810_7_0_0; -.
DR OrthoDB; 9803238at2; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000003813; 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: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; IPR028356; UDPglc_DH_euk.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR11374:SF3; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR11374; UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC 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; PIRSF500133; UDPglc_DH_euk; 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|PIRSR:PIRSR500133-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003813}.
FT DOMAIN 327..443
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 85..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 126..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 156..160
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 215..219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 262..268
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 271..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 333..334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
SQ SEQUENCE 458 AA; 49733 MW; F9A8FD76C2E66AF5 CRC64;
MTICCIGAGY VGGPTMAMIA LKAHDITVNV VDMNASRIAA WNSDNLPVYE PGLDEIVKER
RGKNLFFSTD IHASIAKADI IFVSVNTPTK TYGVGAGRAA DLRYIESVAR TIAEAATTPK
IIVEKSTIPV RTAETIQAIL KANGNGSSHQ VLSNPEFLAE GTAVADLQNP DRVLIGGERT
PEGQQAVETL VSVYARWVPR ERIITTNLWS SELSKLVANA FLAQRISSIN AISALCEATG
ANVDEVAHAI GRDSRIGPKF LKASVGFGGS CFQKDILNLV YLCEYFGLPE VASYWDQVIK
INEFQKHRFA AKIVRTLFNT VAGKKIAVLG FAFKKDTNDT RESPAISVVR DLLEEQANVV
VYDPKVPAEK IRIDVLGSPE TGDRKPEASR LSVASSAYEA SAGAHAVAIL TEWDEFKTLD
FGKIHASMQK PAFLFDGRNI VDLEKLEKIG FRAYGLGK
//
