UGDH1_SOYBN
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 03-AUG-2022, entry version 131.
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}.
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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.GLYMA08G26520.1; -.
DR PRIDE; Q96558; -.
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; CECLNLP; -.
DR OrthoDB; 915490at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000008827; Chromosome 8.
DR Genevisible; Q96558; GM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 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 PANTHER; PTHR11374; PTHR11374; 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; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52413; SSF52413; 1.
DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
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
