UXS1_PONAB
ID UXS1_PONAB Reviewed; 420 AA.
AC Q5R885;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=UDP-glucuronic acid decarboxylase 1;
DE EC=4.1.1.35;
DE AltName: Full=UDP-glucuronate decarboxylase 1;
DE Short=UGD;
DE Short=UXS-1;
GN Name=UXS1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-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 -!- SUBUNIT: Interacts with AKT1. {ECO:0000250}.
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; CR859869; CAH92025.1; -; mRNA.
DR RefSeq; NP_001126176.1; NM_001132704.1.
DR RefSeq; XP_009235107.1; XM_009236832.1.
DR AlphaFoldDB; Q5R885; -.
DR SMR; Q5R885; -.
DR STRING; 9601.ENSPPYP00000013525; -.
DR GeneID; 100173139; -.
DR KEGG; pon:100173139; -.
DR CTD; 80146; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_3_1; -.
DR InParanoid; Q5R885; -.
DR OrthoDB; 848823at2759; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000001595; Unplaced.
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; IEA:InterPro.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IEA:UniProtKB-EC.
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 Acetylation; Decarboxylase; Glycoprotein; Golgi apparatus; Lyase; Membrane;
KW NAD; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..420
FT /note="UDP-glucuronic acid decarboxylase 1"
FT /id="PRO_0000183271"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..420
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 119..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 231..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 273..277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 290..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 357..361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NBZ7"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 47604 MW; EC8DC0E1B1D02157 CRC64;
MVSKALLRLV SAVNRRRMKL LLGIALLAYV ASVWGNFVNM RSIQENGELK IESKIEEMVE
PLREKIRDLE KSFTQKYPPV KFLSEKDRKR ILITGGAGFV GSHLTDKLMM DGHEVTVVDN
FFTGRKRNVE HWIGHENFEL INHDVVEPLY IEVDQIYHLA SPASPPNYMY NPIKTLKTNT
IGTLNMLGLA KRVGARLLLA STSEVYGDPE VHPQSEDYWG HVNPIGPRAC YDEGKRVAET
MCYAYMKQEG VEVRVARIFN TFGPRMHMND GRVVSNFILQ ALQGEPLTVY GSGSQTRAFQ
YVSDLVNGLV ALMNSNVSSP VNLGNPEEHT ILEFAQLIKN LVGSGSEIQF LSEAQDDPQK
RKPDIKKAKL MLGWEPVVPL EEGLNKAIHY FRKELEYQAN NQYIPKPKPA RIKKGRTRHN