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Database: UniProt
Entry: A0A251S6Q0_HELAN
LinkDB: A0A251S6Q0_HELAN
Original site: A0A251S6Q0_HELAN 
ID   A0A251S6Q0_HELAN        Unreviewed;       480 AA.
AC   A0A251S6Q0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=HannXRQ_Chr15g0473051 {ECO:0000313|EMBL:OTF94526.1},
GN   HanXRQr2_Chr15g0684211 {ECO:0000313|EMBL:KAF5763765.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTF94526.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|EMBL:KAF5763765.1, ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5763765.1};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
RN   [2] {ECO:0000313|EMBL:OTF94526.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Leaves {ECO:0000313|EMBL:OTF94526.1};
RA   Langlade N., Munos S.;
RT   "Sunflower complete genome.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF5763765.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:KAF5763765.1};
RA   Gouzy J., Langlade N., Munos S.;
RT   "Helianthus annuus Genome sequencing and assembly Release 2.";
RL   Submitted (JUN-2020) 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|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; MNCJ02000330; KAF5763765.1; -; Genomic_DNA.
DR   EMBL; CM007904; OTF94526.1; -; Genomic_DNA.
DR   STRING; 4232.A0A251S6Q0; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr15g0684211; CDS:HanXRQr2_Chr15g0684211.1; HanXRQr2_Chr15g0684211.
DR   Gramene; mRNA:HanXRQr2_Chr15g0684211; CDS:HanXRQr2_Chr15g0684211.1; HanXRQr2_Chr15g0684211.
DR   InParanoid; A0A251S6Q0; -.
DR   OMA; CFIAVGT; -.
DR   OrthoDB; 167209at2759; -.
DR   UniPathway; UPA00038; UER00491.
DR   Proteomes; UP000215914; Chromosome 15.
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:SF62; 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:UP000215914}.
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;  53034 MW;  F66CCEA86B8EA835 CRC64;
     MVKICCIGAG YVGGPTMAVI ALKCPDIEVA VVDISVPRIN AWNSDQLPIY EPGLEDVVKQ
     CRGKNLFFST DVEKHVCEAD IVFVSVNTPT KTRGLGAGKA ADLTYWESAA RMIADVSKSD
     KIVVEKSTVP VKTAEAIEKI LTHNSKGINF QILSNPEFLA EGTAIEDLFK PDRVLIGGRE
     TPEGQKAIKT LKDVYAHWVP EENIITTNLW SAELSKLAAN AFLAQRISSV NAMSALCEAT
     GANVTEVSYA VGKDTRIGSK FLNPSVGFGG SCFQKDILNL VYICECNGLP EVAEYWRQVI
     KINDYQKSRF VNRIVASMFN TVSNKKIAVL GFAFKKDTGD TRETPAIDVC KGLLGDKARL
     SIYDPQVTED QIQRDLSMNK FDWDHPLHLQ PMSPSTVKQV SVVWDAYAAT KDAHGVCILT
     EWNEFKTLDF QKIYDNMQKP AFIFDGRNVV DAEKLREIGF IVYSIGKPLD AWLKDMPAVA
//
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