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Database: UniProt
Entry: K0RR38_THAOC
LinkDB: K0RR38_THAOC
Original site: K0RR38_THAOC 
ID   K0RR38_THAOC            Unreviewed;       357 AA.
AC   K0RR38;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE            EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN   ORFNames=THAOC_25481 {ECO:0000313|EMBL:EJK54854.1};
OS   Thalassiosira oceanica (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK54854.1, ECO:0000313|Proteomes:UP000266841};
RN   [1] {ECO:0000313|EMBL:EJK54854.1, ECO:0000313|Proteomes:UP000266841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK54854.1,
RC   ECO:0000313|Proteomes:UP000266841};
RX   PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA   Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA   Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA   Rosenstiel P., Hippler M., Laroche J.;
RT   "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT   limitation.";
RL   Genome Biol. 13:R66-R66(2012).
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:EJK54854.1}.
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DR   EMBL; AGNL01035167; EJK54854.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0RR38; -.
DR   EnsemblProtists; EJK54854; EJK54854; THAOC_25481.
DR   eggNOG; KOG1429; Eukaryota.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000266841; 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: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; IPR001763; Rhodanese-like_dom.
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.
DR   PROSITE; PS50206; RHODANESE_3; 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:UP000266841};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          55..103
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   357 AA;  39830 MW;  44283C681FC85112 CRC64;
     MAEDNPGIVR KMSLESGDSP EAKRARVERF VADQQLLASQ SIPTPHTPQV IRTVRLPDSK
     RKKILVTGGS GFVGSHLVDR LMSEGHEVVV LDNFFTGRKA NVEHWLQHPN FSLVRHDVTQ
     PILLEVDQIY HLACPASPPH YQYNPVKTIK TSTMGTINML GLAKRVKARI LLASTSEIYG
     DPQVHPQPES YWGNVNTIGI RACYDEGKRV AETMMYAYKN QNNVDVRVAR IFGDGTQTRS
     FQYVDDLVNG LMKLMNGSYD MPVNIGNPDE YSIADFATKI RDMCESKSEV QFLPKVADDP
     TQRKADISTA KREIDWEPKV SVEEGLKRTI QYFKGEVEAA GEIVPTGPDA SKPKGGD
//
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