UGDH_CAEEL
ID UGDH_CAEEL Reviewed; 481 AA.
AC Q19905;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=UDP-glucose 6-dehydrogenase;
DE Short=UDP-Glc dehydrogenase;
DE Short=UDP-GlcDH;
DE Short=UDPGDH;
DE EC=1.1.1.22 {ECO:0000269|PubMed:12391315};
DE AltName: Full=Squashed vulva protein 4;
GN Name=sqv-4; ORFNames=F29F11.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF ARG-353.
RX PubMed=12391315; DOI=10.1073/pnas.172522499;
RA Hwang H.Y., Horvitz H.R.;
RT "The Caenorhabditis elegans vulval morphogenesis gene sqv-4 encodes a UDP-
RT glucose dehydrogenase that is temporally and spatially regulated.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14224-14229(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=17913784; DOI=10.1242/dev.011361;
RA Bembenek J.N., Richie C.T., Squirrell J.M., Campbell J.M., Eliceiri K.W.,
RA Poteryaev D., Spang A., Golden A., White J.G.;
RT "Cortical granule exocytosis in C. elegans is regulated by cell cycle
RT components including separase.";
RL Development 134:3837-3848(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of caenorhabditis elegans udp-glucose dehydrogenase.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of glycosaminoglycans;
CC hyaluronan, chondroitin sulfate, and heparan sulfate.
CC {ECO:0000269|PubMed:12391315}.
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:0000269|PubMed:12391315};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for UDP-glucose at 22 degrees Celsius
CC {ECO:0000269|PubMed:12391315};
CC KM=0.2 mM for NAD(+)at 22 degrees Celsius
CC {ECO:0000269|PubMed:12391315};
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:0000305|PubMed:12391315}.
CC -!- INTERACTION:
CC Q19905; Q19905: sqv-4; NbExp=3; IntAct=EBI-320696, EBI-320696;
CC -!- TISSUE SPECIFICITY: Expressed in the vulva and in oocytes.
CC {ECO:0000269|PubMed:12391315}.
CC -!- DEVELOPMENTAL STAGE: Expression increases in a subset of vulva
CC precursor cells during middle and late L4 larval stage.
CC {ECO:0000269|PubMed:12391315}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in the
CC size of cortical granules during the first meiotic division.
CC {ECO:0000269|PubMed:17913784}.
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; AY147932; AAN39842.1; -; mRNA.
DR EMBL; Z73974; CAA98269.1; -; Genomic_DNA.
DR PIR; T21550; T21550.
DR RefSeq; NP_505730.1; NM_073329.7.
DR PDB; 2O3J; X-ray; 1.88 A; A/B/C=1-481.
DR PDB; 6OM8; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J/K/L=1-481.
DR PDBsum; 2O3J; -.
DR PDBsum; 6OM8; -.
DR AlphaFoldDB; Q19905; -.
DR SMR; Q19905; -.
DR BioGRID; 44513; 19.
DR DIP; DIP-24290N; -.
DR IntAct; Q19905; 18.
DR STRING; 6239.F29F11.1; -.
DR EPD; Q19905; -.
DR PaxDb; Q19905; -.
DR PeptideAtlas; Q19905; -.
DR EnsemblMetazoa; F29F11.1.1; F29F11.1.1; WBGene00005022.
DR GeneID; 179484; -.
DR KEGG; cel:CELE_F29F11.1; -.
DR UCSC; F29F11.1.1; c. elegans.
DR CTD; 179484; -.
DR WormBase; F29F11.1; CE05767; WBGene00005022; sqv-4.
DR eggNOG; KOG2666; Eukaryota.
DR GeneTree; ENSGT00390000015355; -.
DR HOGENOM; CLU_023810_7_0_1; -.
DR InParanoid; Q19905; -.
DR OMA; CECLNLP; -.
DR OrthoDB; 915490at2759; -.
DR PhylomeDB; Q19905; -.
DR BRENDA; 1.1.1.22; 1045.
DR Reactome; R-CEL-173599; Formation of the active cofactor, UDP-glucuronate.
DR SignaLink; Q19905; -.
DR UniPathway; UPA00038; UER00491.
DR EvolutionaryTrace; Q19905; -.
DR PRO; PR:Q19905; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00005022; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IDA:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IDA:WormBase.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..481
FT /note="UDP-glucose 6-dehydrogenase"
FT /id="PRO_0000074063"
FT ACT_SITE 283
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 16..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 135..136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 168..172
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 227..231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 274..280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 283..286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O60701"
FT MUTAGEN 353
FT /note="R->H: In n2827; defects in vulva morphogenesis
FT during L4 larval stage."
FT /evidence="ECO:0000269|PubMed:12391315"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6OM8"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2O3J"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6OM8"
FT TURN 103..107
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 175..180
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 220..251
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:2O3J"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 284..297
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 301..328
FT /evidence="ECO:0007829|PDB:2O3J"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 406..410
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:2O3J"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:2O3J"
FT STRAND 461..464
FT /evidence="ECO:0007829|PDB:2O3J"
SQ SEQUENCE 481 AA; 52755 MW; 4E789DC5D6679531 CRC64;
MTDQVFGKVS KVVCVGAGYV GGPTCAMIAH KCPHITVTVV DMNTAKIAEW NSDKLPIYEP
GLDEIVFAAR GRNLFFSSDI PKAIAEADLI FISVNTPTKM YGRGKGMAPD LKYVESVSRT
IAQYAGGPKI VVEKSTVPVK AAESIGCILR EAQKNNENLK FQVLSNPEFL AEGTAMKDLA
NPDRVLIGGE SSPEGLQAVA ELVRIYENWV PRNRIITTNT WSSELSKLVA NAFLAQRISS
INSISAVCEA TGAEISEVAH AVGYDTRIGS KFLQASVGFG GSCFQKDVLS LVYLCESLNL
PQVADYWQGV ININNWQRRR FADKIIAELF NTVTDKKIAI FGFAFKKNTG DTRESSAIHV
IKHLMEEHAK LSVYDPKVQK SQMLNDLASV TSAQDVERLI TVESDPYAAA RGAHAIVVLT
EWDEFVELNY SQIHNDMQHP AAIFDGRLIL DQKALREIGF RTFAIGTSPD QAYNLFGTAG
Y
