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Database: UniProt/TrEMBL
Entry: Q1ARF7_RUBXD
LinkDB: Q1ARF7_RUBXD
Original site: Q1ARF7_RUBXD 
ID   Q1ARF7_RUBXD            Unreviewed;       322 AA.
AC   Q1ARF7;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE            EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN   OrderedLocusNames=Rxyl_3114 {ECO:0000313|EMBL:ABG06021.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG06021.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG06021.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) 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}.
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DR   EMBL; CP000386; ABG06021.1; -; Genomic_DNA.
DR   RefSeq; WP_011566026.1; NC_008148.1.
DR   AlphaFoldDB; Q1ARF7; -.
DR   STRING; 266117.Rxyl_3114; -.
DR   KEGG; rxy:Rxyl_3114; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_4_0_11; -.
DR   OrthoDB; 9801785at2; -.
DR   PhylomeDB; Q1ARF7; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000006637; Chromosome.
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   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:UP000006637};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          9..306
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   322 AA;  36170 MW;  B6E52EC14A0DEED3 CRC64;
     MPEGRRRALV TGGAGFIGSH LCDRLVSEGY AVVCMDNLRT GSLRNIAHLR SEPRFEYVDH
     DVTSYIRVPG RLDEVYHFAS PASPKDFERI PIPILKVGAL GTHNALGLSL AKGARFMLAS
     TSEVYGDPLV HPQPEDYWGN VNPIGVRGVY DEAKRYAEAI TMAYHRHHGL DTRIVRIFNT
     YGPRMRPDDG RMIPNFISQA LSGRPLTVYG DGSQTRSVQY IDDLVEGIFR LMRSEERRPV
     NIGNPVEYTV REVAELVLRL SGSRAGISFR PLPKDDPKQR CPDITRAREV LGWEPRVPAE
     EGLRRTLEWF SGHVHRAGEK TG
//
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