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Database: UniProt
Entry: A0A0V1N376_9BILA
LinkDB: A0A0V1N376_9BILA
Original site: A0A0V1N376_9BILA 
ID   A0A0V1N376_9BILA        Unreviewed;       712 AA.
AC   A0A0V1N376;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE            EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
DE   Flags: Fragment;
GN   Name=UXS1 {ECO:0000313|EMBL:KRZ78449.1};
GN   ORFNames=T10_3206 {ECO:0000313|EMBL:KRZ78449.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ78449.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ78449.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ78449.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00034228};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23917;
CC         Evidence={ECO:0000256|ARBA:ARBA00034228};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000256|ARBA:ARBA00001911};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-xylose
CC       biosynthesis; UDP-alpha-D-xylose from UDP-alpha-D-glucuronate: step
CC       1/1. {ECO:0000256|ARBA:ARBA00005100}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004447}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. UDP-glucuronic acid decarboxylase subfamily.
CC       {ECO:0000256|ARBA:ARBA00007505}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ78449.1}.
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DR   EMBL; JYDO01000012; KRZ78449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1N376; -.
DR   STRING; 268474.A0A0V1N376; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; 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   CDD; cd05230; UGD_SDR_e; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR003958; CBFA_NFYB_domain.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR044516; UXS.
DR   PANTHER; PTHR43078:SF6; UDP-GLUCURONIC ACID DECARBOXYLASE 1; 1.
DR   PANTHER; PTHR43078; UDP-GLUCURONIC ACID DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR   Pfam; PF16363; GDP_Man_Dehyd; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Lyase {ECO:0000256|ARBA:ARBA00022793};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          9..66
FT                   /note="Transcription factor CBF/NF-Y/archaeal histone"
FT                   /evidence="ECO:0000259|Pfam:PF00808"
FT   DOMAIN          202..488
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
FT   COILED          142..169
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         712
FT                   /evidence="ECO:0000313|EMBL:KRZ78449.1"
SQ   SEQUENCE   712 AA;  80426 MW;  70C74DCDEF4C03E6 CRC64;
     MEDSIISTSR VRTIMKSSPD VTNISSEAVY CMGKVAELFV VTLARRAAEQ ANDAGEVTYE
     HVAECVQNDM RMFYLHEVIP RKMKVSDIPG LDISDLQMTD EKSIWFYRRN CNGDQLGHFL
     INNNNNIRSD EGIEQGDSRQ TLQAFLKELN ILKNTVDTQR NEIDLLRKEI AVGKGLQHPA
     ILNSSRYPRV KFRNFTEKKR ILITGGSGFV GSHLVDQLLL DGHQVICVDN HFTGQKRNIE
     HWIGHPNFEL ISHDISNPLY LTVDQIYHLA SPASPPHYMF NPVKTIKTNT LGTINVLGLA
     RRNRAKILLA STSEVYGDPV VHPQPETYWG NVNPIGPRSC YDEGKRVAEA LMVAYHKQEA
     VDIRIARIFN TFGPRMNMND GRVVSNFILQ ALENRSITVY GSGQHTRSFQ YVSDLVSGLI
     KLMESNVTVP VNFGNPEEYT IAEFALMVKN LTKCKCKIVH HQSSVDDPQR RKPNITRAWQ
     LLQWKPKYDY RVPPMSQHPF SISYHPFPGR NGVVLSPQFP LTHQFSNGLQ YGSGGGYYQR
     GRLNIPFLKW GAIWNKRSLL TAGGNAPWYN YGHMVQPTNS LGLRPAEITK MMMDPLFNEA
     RITKSGRVPI PVSNLPGDYN PAYCQPPFCN PFTHTFGIGI MHQESKNFEI DGLLDFPVPT
     GSFGQGIRFP LSGNGYFGPF PASLFYGHHV HPVNPFPLLG KDWLAKAKLL TR
//
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