ID A0A1T1BN45_9FLAO Unreviewed; 312 AA.
AC A0A1T1BN45;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-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=BXU10_16660 {ECO:0000313|EMBL:OOV17692.1};
OS Flavobacterium sp. LM4.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1938609 {ECO:0000313|EMBL:OOV17692.1, ECO:0000313|Proteomes:UP000190722};
RN [1] {ECO:0000313|EMBL:OOV17692.1, ECO:0000313|Proteomes:UP000190722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM4 {ECO:0000313|EMBL:OOV17692.1,
RC ECO:0000313|Proteomes:UP000190722};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OOV17692.1}.
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DR EMBL; MUFW01000002; OOV17692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1BN45; -.
DR STRING; 1938609.BXU10_16660; -.
DR OrthoDB; 9801785at2; -.
DR UniPathway; UPA00796; UER00771.
DR Proteomes; UP000190722; Unassembled WGS sequence.
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:ARBA00023239};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 7..302
FT /note="NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF16363"
SQ SEQUENCE 312 AA; 35393 MW; 30E699444C4C9D13 CRC64;
MSRKKILITG GAGFVGSHLC DRLLNEGNEV YCLDNFFTGQ KQNVVHLLDN PYFELIRHDV
TAPFFIETDE IYNLACPASP IHYQYNAIKT MKTSVMGAIN MLGLAKRVNA KILQASTSEV
YGDPLVHPQP ESYWGHVNPI GERSCYDEGK RSAETLFLNY HKQNNVKIKI IRIFNTYGPR
MHPNDGRVVS NFIVQALQNQ DITVYGQGNQ TRSFQYVDDL VEGMIRLMNS KDSFTGPVNV
GNPNEFTILE LAEKIIQLTD SKSKIIYKPL PSDDPMQRQP DISLAKKELD WSPKINLDEG
LIKTIDYFKS II
//