ID B4FAG0_MAIZE Unreviewed; 350 AA.
AC B4FAG0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN Name=100191862 {ECO:0000313|EnsemblPlants:Zm00001eb012580_P001};
GN ORFNames=ZEAMMB73_Zm00001d028653 {ECO:0000313|EMBL:ONL96639.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF79103.1};
RN [1] {ECO:0000313|EMBL:ACF79103.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACF79103.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [2] {ECO:0000313|EMBL:ONL96639.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb012580_P001,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONL96639.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb012580_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb012580_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00025005}.
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 -!- 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; BT034098; ACF79103.1; -; mRNA.
DR EMBL; BT063387; ACN28084.1; -; mRNA.
DR EMBL; BT064421; ACN29118.1; -; mRNA.
DR EMBL; BT067527; ACN34424.1; -; mRNA.
DR EMBL; CM007647; ONL96639.1; -; Genomic_DNA.
DR EMBL; CM007647; ONL96641.1; -; Genomic_DNA.
DR EMBL; CM007647; ONL96643.1; -; Genomic_DNA.
DR RefSeq; NP_001130758.1; NM_001137286.1.
DR RefSeq; XP_008672856.1; XM_008674634.1.
DR AlphaFoldDB; B4FAG0; -.
DR SMR; B4FAG0; -.
DR IntAct; B4FAG0; 12.
DR STRING; 4577.B4FAG0; -.
DR PaxDb; 4577-GRMZM2G044027_P01; -.
DR EnsemblPlants; Zm00001eb012580_T001; Zm00001eb012580_P001; Zm00001eb012580.
DR EnsemblPlants; Zm00001eb012580_T002; Zm00001eb012580_P002; Zm00001eb012580.
DR GeneID; 100191862; -.
DR Gramene; Zm00001eb012580_T001; Zm00001eb012580_P001; Zm00001eb012580.
DR Gramene; Zm00001eb012580_T002; Zm00001eb012580_P002; Zm00001eb012580.
DR KEGG; zma:100191862; -.
DR eggNOG; KOG1429; Eukaryota.
DR HOGENOM; CLU_007383_4_0_1; -.
DR InParanoid; B4FAG0; -.
DR OMA; TISEVWH; -.
DR OrthoDB; 5491077at2759; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B4FAG0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0048040; F:UDP-glucuronate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042732; P:D-xylose metabolic process; IBA:GO_Central.
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; 2.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR044516; UXS.
DR PANTHER; PTHR43078:SF42; UDP-GLUCURONATE DECARBOXYLASE; 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 1: Evidence at protein level;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00022793};
KW Proteomics identification {ECO:0007829|PeptideAtlas:B4FAG0};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 38..331
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 39310 MW; 231CDC2A06358264 CRC64;
MAQKETNGSN GEHISTRPPP TPSPLRFSKF FQANLRILVT GGAGFIGSHL VDRLMENEKH
EVIVADNFFT GSKDNLKKWI GHPRFELIRH DVTEPLLVEV DQIYHLACPA SPIFYKHNPV
KTIKTNVIGT LNMLGLAKRV GARILLTSTS EVYGDPLEHP QTEAYWGNVN PIGVRSCYDE
GKRVAETLMF DYHRQHGIEI RIARIFNTYG PRMNIDDGRV VSNFIAQAVR GEPLTVQKPG
TQTRSFCYVA DMVDGLIRLM NGNNTGPINL GNPGEFTMLE LAENVKELIN PDITVTMTEN
TPDDPRQRKP DITKAKEVLG WEPKIVLKDG LVLMEDDFRE RLAVPKKTKA
//
