ID D6E923_9ACTN Unreviewed; 402 AA.
AC D6E923;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
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 ORFNames=GPA_17490 {ECO:0000313|EMBL:CBL04220.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04220.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL04220.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL04220.1, ECO:0000313|Proteomes:UP000008805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; FP929047; CBL04220.1; -; Genomic_DNA.
DR RefSeq; WP_015539569.1; NC_021021.1.
DR AlphaFoldDB; D6E923; -.
DR KEGG; gpa:GPA_17490; -.
DR PATRIC; fig|657308.3.peg.1312; -.
DR HOGENOM; CLU_023810_2_0_11; -.
DR BioCyc; GPAM657308:GPA_RS08165-MONOMER; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000008805; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
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:SF2; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR43750; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008805}.
FT DOMAIN 314..401
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-1"
FT BINDING 29
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 88
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 123
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 147..150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 252..256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
FT BINDING 328
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-3"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500134-2"
SQ SEQUENCE 402 AA; 43535 MW; C527DB783E83C834 CRC64;
MRIAVAGTGY VGLSLAVLLA RGSEVVAVDV VPAKVEALAR WESPIRDAEI EEALAGAASG
ERPLALSATL DAGEGYRNID FAVVATPTDY DPARNFFNTS SVEAAVAAIR AASPEAWIVV
KSTVPVGYTA QLRERLGDRR ILFSPEFLRE GRALHDNLHP SRIIVGADES DPESMEAARR
FANLLAEGAE DEAPVLVMGS TEAEAVKLFA NTFLALRVAY FNELDTYASS RGLDAARVIE
GVCLDPRVGS HYNNPSFGYG GYCLPKDTKQ LLANYADVPQ NVMGAVVDAN RTRKDFVADQ
VLERASALEE PLVGVYRLTM KTGSDNFRAS SVQGVMKRVK AKGVPVLVYE PTLSAPEFFG
SEVTHDLESF KERAGVIVAN RWSDELADVV GKVYTRDLFK RD
//
