UXS1_XENTR
ID UXS1_XENTR Reviewed; 421 AA.
AC Q6DF08;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE EC=4.1.1.35;
DE AltName: Full=UDP-glucuronate decarboxylase 1;
DE Short=UXS-1;
GN Name=uxs1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD-dependent decarboxylation of UDP-glucuronic
CC acid to UDP-xylose. Necessary for the biosynthesis of the core
CC tetrasaccharide in glycosaminoglycan biosynthesis (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + UDP-alpha-D-glucuronate = CO2 + UDP-alpha-D-xylose;
CC Xref=Rhea:RHEA:23916, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58052; EC=4.1.1.35;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
CC biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
CC 1/1.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. UDP-glucuronic acid decarboxylase subfamily. {ECO:0000305}.
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DR EMBL; BC076935; AAH76935.1; -; mRNA.
DR RefSeq; NP_001006849.1; NM_001006848.1.
DR AlphaFoldDB; Q6DF08; -.
DR SMR; Q6DF08; -.
DR PaxDb; Q6DF08; -.
DR DNASU; 448599; -.
DR Ensembl; ENSXETT00000066772; ENSXETP00000098487; ENSXETG00000021671.
DR GeneID; 448599; -.
DR KEGG; xtr:448599; -.
DR CTD; 80146; -.
DR Xenbase; XB-GENE-997577; uxs1.
DR eggNOG; KOG1429; Eukaryota.
DR InParanoid; Q6DF08; -.
DR OrthoDB; 848823at2759; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000021671; Expressed in brain and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:InterPro.
DR GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044516; UXS.
DR InterPro; IPR021761; UXS1_N.
DR PANTHER; PTHR43078; PTHR43078; 1.
DR Pfam; PF16363; GDP_Man_Dehyd; 1.
DR Pfam; PF11803; UXS1_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Glycoprotein; Golgi apparatus; Lyase; Membrane; NAD;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..421
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000183274"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..421
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 400..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 232
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 120..145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232..236
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 274..278
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 291..298
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 358..362
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 47875 MW; 5AAC42C512674852 CRC64;
MVRTRIQRLL TGINRRMMKL LIALALIAYV ASVWGNFVNM SKSIQENGEQ KMEKKIEEVI
APLREKIQNL ERSFTQKYPP VKFLSEKDRK RILITGGAGF VGSHLTDKLM MDGHEVTVVD
NFFTGRKRNV EHWIGHENFE LINHDVVEPL YIEVDQIYHL ASPASPPNYM YNPIKTLKTN
TIGTLNMLGL AKRVGARLLL ASTSEVYGDP EVHPQSEEYW GHVNPIGPRA CYDEGKRVAE
TMCYAYMKQE GVEVRVARIF NTFGPRMHMN DGRVVSNFIL QALQGEQLTV YGSGEQTRAF
QYVSDLVNGL VALMNSNVSS PVNLGNPQEH SIVQFARLIK QLVGSGGEIS FLSEAQDDPQ
RRKPDIRKAK LLLGWEPVVP LEEGLNKTIH YFRKELEHQA NNQYIPKPKP ARVKKGRTRH
N
