ID A0A3Q2HAS3_HORSE Unreviewed; 453 AA.
AC A0A3Q2HAS3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=UGDH {ECO:0000313|Ensembl:ENSECAP00000030404.1,
GN ECO:0000313|VGNC:VGNC:24775};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000030404.1, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000030404.1, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030404.1,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000030404.1}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030404.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
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 AlphaFoldDB; A0A3Q2HAS3; -.
DR Ensembl; ENSECAT00000043403.2; ENSECAP00000030404.1; ENSECAG00000015009.4.
DR VGNC; VGNC:24775; UGDH.
DR GeneTree; ENSGT00390000015355; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000002281; Chromosome 3.
DR Bgee; ENSECAG00000015009; Expressed in adult mammalian kidney and 23 other cell types or tissues.
DR ExpressionAtlas; A0A3Q2HAS3; baseline.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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:SF59; 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 1: Evidence at protein level;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000124};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000124};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A3Q2HAS3};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT DOMAIN 291..406
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT REGION 434..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT BINDING 48..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 89..90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 120..124
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 124
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 179..183
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 226..232
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 235..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 297..298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
FT BINDING 305
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-2"
SQ SEQUENCE 453 AA; 50724 MW; 24EC1942CE909B56 CRC64;
MLWMLFAPSP LRRPGLKEVV ESCRGKNLFF STNIDDAINE ADLVFISVNT PTKTYGMGKG
RAADLKYIEA CARRIVQNSH GYKIVTEKST VPVRAAESIR RIFDANTKPN LNLQVLSNPE
FLAEGTAIKD LKNPDRVLIG GDETPEGQRA VQALCAVYEH WVPREKILTT NTWSSELSKL
AANAFLAQRI SSINSISALC EATGADVEEV ATAIGMDQRI GNKFLKASVG FGGSCFQKDV
LNLVYLCEAL NLPEVARYWQ QVIDMNDYQR RRFASRIIDS LFNTVTDKKI AILGFAFKKD
TGDTRESSSI YISKYLMDEG AHLHIYDPKV PREQIVVDLS HPGVSEDDQV SRLVTISKDP
YEACDGAHAV VICTEWDMFK ELDYERIHKK MLKPAFIFDG RRVLDGLHNE LQTIGFQIET
IGKKVSSKRI PYAPSGEIPK FSLQDPPNKK PKV
//
