ID A0A364RD68_9BACT Unreviewed; 323 AA.
AC A0A364RD68;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN ORFNames=DP923_10510 {ECO:0000313|EMBL:RAU82219.1};
OS Pontibacter arcticus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=2080288 {ECO:0000313|EMBL:RAU82219.1, ECO:0000313|Proteomes:UP000251692};
RN [1] {ECO:0000313|EMBL:RAU82219.1, ECO:0000313|Proteomes:UP000251692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2b14 {ECO:0000313|EMBL:RAU82219.1,
RC ECO:0000313|Proteomes:UP000251692};
RA Liu Z.-W.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAU82219.1, ECO:0000313|Proteomes:UP000251692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2b14 {ECO:0000313|EMBL:RAU82219.1,
RC ECO:0000313|Proteomes:UP000251692};
RA Du Z.-J.;
RT "Pontibacter sp. 2b14 genomic sequence and assembly.";
RL Submitted (JUL-2018) 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:RAU82219.1}.
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DR EMBL; QMDV01000003; RAU82219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364RD68; -.
DR OrthoDB; 9810015at2; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000251692; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 CDD; cd05230; UGD_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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; PF16363; GDP_Man_Dehyd; 1.
DR PRINTS; PR01713; NUCEPIMERASE.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
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:UP000251692};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 7..304
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 323 AA; 36616 MW; F7164607E02E55CB CRC64;
MVKKRVLITG GAGFLGSHLC DRFIKEGYHV IAMDNLITGN LENIEHLFKL PNFEFYHHDV
SKFVHVPGHL DYILHFASPA SPIDYLKIPI QTLKVGSLGT HNLLGLAKAK NARMLIASTS
EVYGDPQIHP QPEDYWGNVN PVGPRGCYDE AKRFQEAMTM AYHMHHGLET RIVRIFNTYG
PRMRLNDGRV LPAFLSQALR GEPLSIFGDG SQTRSFCYVD DLVEGIYRLL LSDYALPVNV
GNPSEITIKE FAEEICKLTG VELKLEYQPL PKDDPQMRRP DIAKAQEILG WEPKVDRAEG
LKRTLEYFKE KVPVAPKENL NFK
//
