ID UGDH1_SOYBN Reviewed; 480 AA. AC Q96558; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 139. DE RecName: Full=UDP-glucose 6-dehydrogenase 1; DE Short=UDP-Glc dehydrogenase 1; DE Short=UDP-GlcDH 1; DE Short=UDPGDH 1; DE EC=1.1.1.22; DE AltName: Full=Gm-UGD1; GN Name=UGD1; OS Glycine max (Soybean) (Glycine hispida). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine; OC Glycine subgen. Soja. OX NCBI_TaxID=3847; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=cv. Williams 82; RX PubMed=8938413; DOI=10.1104/pp.112.3.1127; RA Tenhaken R., Thulke O.; RT "Cloning of an enzyme that synthesizes a key nucleotide-sugar precursor of RT hemicellulose biosynthesis from soybean: UDP-glucose dehydrogenase."; RL Plant Physiol. 112:1127-1134(1996). RN [2] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=18057039; DOI=10.1093/jxb/erm209; RA Klinghammer M., Tenhaken R.; RT "Genome-wide analysis of the UDP-glucose dehydrogenase gene family in RT Arabidopsis, a key enzyme for matrix polysaccharides in cell walls."; RL J. Exp. Bot. 58:3609-3621(2007). CC -!- FUNCTION: Involved in the biosynthesis of UDP-glucuronic acid (UDP- CC GlcA), providing nucleotide sugars for cell-wall polymers. CC {ECO:0000269|PubMed:8938413}. 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 -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step CC 1/1. CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U53418; AAB58398.1; -; mRNA. DR PIR; T08818; T08818. DR RefSeq; NP_001238410.1; NM_001251481.1. DR RefSeq; XP_006584641.1; XM_006584578.2. DR AlphaFoldDB; Q96558; -. DR SMR; Q96558; -. DR STRING; 3847.Q96558; -. DR PaxDb; 3847-GLYMA08G26520-1; -. DR ProMEX; Q96558; -. DR EnsemblPlants; KRH44990; KRH44990; GLYMA_08G243000. DR GeneID; 548074; -. DR Gramene; KRH44990; KRH44990; GLYMA_08G243000. DR KEGG; gmx:548074; -. DR eggNOG; KOG2666; Eukaryota. DR HOGENOM; CLU_023810_7_0_1; -. DR InParanoid; Q96558; -. DR OMA; CFIAVGT; -. DR OrthoDB; 167209at2759; -. DR UniPathway; UPA00038; UER00491. DR Proteomes; UP000008827; Chromosome 8. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0006024; P:glycosaminoglycan biosynthetic process; IBA:GO_Central. 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. DR Genevisible; Q96558; GM. PE 2: Evidence at transcript level; KW NAD; Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1..480 FT /note="UDP-glucose 6-dehydrogenase 1" FT /id="PRO_0000074065" FT ACT_SITE 272 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT BINDING 8..13 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 33 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 38 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 86..90 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 127..128 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 157..161 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 161 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 216..223 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 256..269 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 272..275 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 334..335 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 342 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 447 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 393 FT /note="Phosphoserine" FT /evidence="ECO:0000250" SQ SEQUENCE 480 AA; 52942 MW; AFCADA0F5951FD11 CRC64; MVKICCIGAG YVGGPTMAVI ALKCPSIEVA VVDISKSRIA AWNSDQLPIY EPGLDGVVKQ CRGKNLFFST DVEKHVFEAD IVFVSVNTPT KTQGLGAGKA ADLTYWESAA RMIADVSKSD KIVVEKSTVP VKTAEAIEKI LTHNSKGIKF QILSNPEFLA EGTAIKDLFN PDRVLIGGRE TPEGQKAIQT LKDVYAQWVP EERILTTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT GANVQQVSYS VGTDSRIGPK FLNASVGFGG SCFQKDILNL VYICECNGLP EVAEYWKQVI KINDYQKSRF VNRVVASMFN TVSNKKIAIL GFAFKKDTGD TRETPAIDVC QGLLGDKANL SIYDPQVTED QIQRDLSMNK FDWDHPIHLQ PTSPTTVKKV SVVWDAYEAT KDAHGLCILT EWDEFKTLDY QKIFDNMQKP AFVFDGRNIV DADKLREIGF IVYSIGKPLD PWLKDMPAVA //