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Database: UniProt
Entry: A0A3Q7H0L9_SOLLC
LinkDB: A0A3Q7H0L9_SOLLC
Original site: A0A3Q7H0L9_SOLLC 
ID   A0A3Q7H0L9_SOLLC        Unreviewed;       480 AA.
AC   A0A3Q7H0L9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Name=101259257 {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1};
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1};
RN   [1] {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Heinz 1706
RC   {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1};
RX   PubMed=22660326; DOI=10.1038/nature11119;
RG   Tomato Genome Consortium;
RT   "The tomato genome sequence provides insights into fleshy fruit
RT   evolution.";
RL   Nature 485:635-641(2012).
RN   [2] {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1}
RP   IDENTIFICATION.
RC   STRAIN=cv. Heinz 1706
RC   {ECO:0000313|EnsemblPlants:Solyc06g069550.1.1.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2019) to UniProtKB.
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|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   RefSeq; XP_010322576.1; XM_010324274.1.
DR   AlphaFoldDB; A0A3Q7H0L9; -.
DR   STRING; 4081.A0A3Q7H0L9; -.
DR   PaxDb; 4081-Solyc06g069550-1-1; -.
DR   EnsemblPlants; Solyc06g069550.1.1; Solyc06g069550.1.1.1; Solyc06g069550.1.
DR   GeneID; 101259257; -.
DR   Gramene; Solyc06g069550.1.1; Solyc06g069550.1.1.1; Solyc06g069550.1.
DR   KEGG; sly:101259257; -.
DR   InParanoid; A0A3Q7H0L9; -.
DR   OMA; IAFKCPA; -.
DR   OrthoDB; 167209at2759; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000004994; Chromosome 6.
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:SF50; 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|PIRNR:PIRNR000124};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004994}.
FT   DOMAIN          328..452
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   ACT_SITE        272
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         86..90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         127..128
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         272..275
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT   BINDING         342
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
SQ   SEQUENCE   480 AA;  52930 MW;  F008E8E7C98ED768 CRC64;
     MVKICCIGAG YVGGPTMAVI AFKCPAIEVA VVDISFARIT AWNSDQLPIY EPGLEDIVKQ
     CRGKNLFFST EVEKHVSEAD IIFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSKND
     KIVVEKSTVP VKTAEAIEKI LTHNSNGIKY QILSNPEFLA EGTAIQDLFN PDRILIGGRE
     TPGGQKAIQA LKEVYAHWVP EDRIICTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT
     GADVTQVSHA VGKDTRVGSK FLNASVGFGG SCFQKDILSL VYICECNGLK EVANYWKQVI
     QVNDYQKNRF VNRVVSSMFN TVSGKKIAIL GFAFKKDTGD TRETPAIDVC KGLLGDNANL
     SIYDPQVTED QIRKDLSMKK FDWDNPIHLQ PMSPTVMKQL NVVWDAYAAT KGAHGLCLLT
     EWDEFKTLDF KKIYDNMQKP AFVFDGRNIV DEQKLREIGF IVYSIGKPLD GWLKDMPAVA
//
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