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}.
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; 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
//