ID A0A1M6D0X6_9FLAO Unreviewed; 329 AA.
AC A0A1M6D0X6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=UDP-glucuronate decarboxylase {ECO:0000256|ARBA:ARBA00012290};
DE EC=4.1.1.35 {ECO:0000256|ARBA:ARBA00012290};
GN ORFNames=SAMN04488096_103248 {ECO:0000313|EMBL:SHI66870.1};
OS Mesonia phycicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mesonia.
OX NCBI_TaxID=579105 {ECO:0000313|EMBL:SHI66870.1, ECO:0000313|Proteomes:UP000184225};
RN [1] {ECO:0000313|EMBL:SHI66870.1, ECO:0000313|Proteomes:UP000184225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21425 {ECO:0000313|EMBL:SHI66870.1,
RC ECO:0000313|Proteomes:UP000184225};
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; FQYY01000003; SHI66870.1; -; Genomic_DNA.
DR RefSeq; WP_073149219.1; NZ_FQYY01000003.1.
DR AlphaFoldDB; A0A1M6D0X6; -.
DR STRING; 579105.SAMN04488096_103248; -.
DR OrthoDB; 9801785at2; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000184225; 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:UP000184225};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 6..303
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 329 AA; 37589 MW; B389090EAA39A876 CRC64;
MAKRVLITGA AGFLGSHLCD KFIANGFYVI GMDNLITGDL KNIEHLFGLE NFEFHHHDVT
KFVHIGGDLD YILHFASPAS PIDYLKIPIQ TLKVGSLGTH NLLGLAKEKD ARILIASTSE
VYGDPLVHPQ SEEYFGNVNT ISPRGVYDEA KRFQESITMA YHRFHRLETR IVRIFNTYGP
RMRLNDGRVI PAFIGQALRG ENLTIFGDGS QTRSFCYVDD QIDGIYKLLF SDYTNPINIG
NPHEITIKEF AQEIVNLTGT NQKMIFKELP QDDPKQRKPD ITKAKNILNW EPKVSREEGM
KKTYEYFKAL SPQELEKKEH KDFSNHIRK
//