ID E3MQX3_CAERE Unreviewed; 481 AA.
AC E3MQX3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00015132, ECO:0000256|PIRNR:PIRNR000124};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954, ECO:0000256|PIRNR:PIRNR000124};
GN Name=Cre-sqv-4 {ECO:0000313|EMBL:EFP07064.1};
GN ORFNames=CRE_12910 {ECO:0000313|EMBL:EFP07064.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans;
CC hyaluronan, chondroitin sulfate, and heparan sulfate.
CC {ECO:0000256|PIRNR:PIRNR000124}.
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; DS268467; EFP07064.1; -; Genomic_DNA.
DR RefSeq; XP_003101465.1; XM_003101417.1.
DR AlphaFoldDB; E3MQX3; -.
DR STRING; 31234.E3MQX3; -.
DR EnsemblMetazoa; CRE12910.1; CRE12910.1; WBGene00065019.
DR GeneID; 9799826; -.
DR KEGG; crq:GCK72_016462; -.
DR CTD; 9799826; -.
DR eggNOG; KOG2666; Eukaryota.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; E3MQX3; -.
DR OMA; CFIAVGT; -.
DR OrthoDB; 167209at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
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:0018991; P:egg-laying behavior; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:EnsemblMetazoa.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0040025; P:vulval development; IEA:EnsemblMetazoa.
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.
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:UP000008281}.
FT DOMAIN 339..452
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT BINDING 16..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 94..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 135..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 168..172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 227..231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 274..280
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 283..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
SQ SEQUENCE 481 AA; 52912 MW; 5303C0C5B3011812 CRC64;
MTDQVFGKVS KVVCVGAGYV GGPTCAMIAH KCPHITVTVV DMNTAKIAEW NSDKLPIYEP
GLDEIVFAAR DRNLFFSSDI PKAIAEADLI FISVNTPTKM YGRGKGMAPD LKYVESVSRT
IAQYAVGPKI VVEKSTVPVK AAESIGCILR EAQKNNENLK FQVLSNPEFL AEGTAMKDLA
NPDRVLIGGE TSPEGLQAVA ELVRIYENWV PRDRIITTNT WSSELSKLVA NAFLAQRISS
INSISAVCEA TGAEISEVAH AVGFDTRIGS KFLKASVGFG GSCFQKDVLS LVYLCESLNL
PQVAEYWQGV INVNNWQRRR FADKIIAELF NTVTDKKIAI FGFAFKKNTG DTRESSAIYV
IKHLMEEHAK LSIYDPKVQK SQMLNDLASV TSADDVSRLI TVETDPYTAA RGAHAIVVLT
EWDEFVELNY TRIHDDMQHP AAIFDGRLIL DQKALRDIGF RTFAIGTSPD QAYNLFGTAG
Y
//
