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Database: UniProt
Entry: A0A1K1P8B4_9FLAO
LinkDB: A0A1K1P8B4_9FLAO
Original site: A0A1K1P8B4_9FLAO 
ID   A0A1K1P8B4_9FLAO        Unreviewed;       328 AA.
AC   A0A1K1P8B4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE            EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN   ORFNames=SAMN02927921_01675 {ECO:0000313|EMBL:SFW43699.1};
OS   Sinomicrobium oceani.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sinomicrobium.
OX   NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW43699.1, ECO:0000313|Proteomes:UP000182248};
RN   [1] {ECO:0000313|EMBL:SFW43699.1, ECO:0000313|Proteomes:UP000182248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW43699.1,
RC   ECO:0000313|Proteomes:UP000182248};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FPJE01000007; SFW43699.1; -; Genomic_DNA.
DR   RefSeq; WP_072316896.1; NZ_JAPPSR010000015.1.
DR   AlphaFoldDB; A0A1K1P8B4; -.
DR   STRING; 1150368.SAMN02927921_01675; -.
DR   OrthoDB; 9801785at2; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000182248; 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   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:UP000182248};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          5..302
FT                   /note="NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF16363"
SQ   SEQUENCE   328 AA;  37542 MW;  B7DDF3EF8E0CCA8E CRC64;
     MDRILITGAA GFIGSHLCDR FANEGFYVIG MDNLITGDMR NIDHLLPRDN FEFHHHDVTK
     FVHISGELDY ILHFASPASP IDYLKIPIQT LKVSSLGIHN LLGLAKDKKA RLLIASTSEV
     YGDPLVHPQS EDYYGNVNTI SPRGVYDEAK RFQESMTMAY HRFHGMETRI ARIFNTYGPR
     MRLNDGRVIP AFIGQALRGE DLTVFGDGSQ TRSFCYIEDQ VEGLYRLLFS DYTDPVNIGN
     PEEISIRDFA GEVIKLTGTD QKIIYKPLPQ DDPMQRQPDI AKAREILGWE PKVNRSEGMR
     KTYEYFKNLP PEELNKKEHK DFSSHIKR
//
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