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Database: UniProt
Entry: A0A3N6PFJ4_9CYAN
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Original site: A0A3N6PFJ4_9CYAN 
ID   A0A3N6PFJ4_9CYAN        Unreviewed;       738 AA.
AC   A0A3N6PFJ4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=D5R40_09565 {ECO:0000313|EMBL:RQH46697.1};
OS   Okeania hirsuta.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Okeania.
OX   NCBI_TaxID=1458930 {ECO:0000313|EMBL:RQH46697.1, ECO:0000313|Proteomes:UP000269154};
RN   [1] {ECO:0000313|EMBL:RQH46697.1, ECO:0000313|Proteomes:UP000269154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAB10Feb10-1 {ECO:0000313|EMBL:RQH46697.1,
RC   ECO:0000313|Proteomes:UP000269154};
RX   PubMed=30444349;
RA   Moss N.A., Leao T., Rankin M., McCullough T.M., Qu P., Korobeynikov A.,
RA   Smith J.L., Gerwick L., Gerwick W.H.;
RT   "Ketoreductase domain dysfunction expands chemodiversity: malyngamide
RT   biosynthesis in the cyanobacterium Okeania hirsuta.";
RL   ACS Chem. Biol. 0:0-0(2018).
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:RQH46697.1}.
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DR   EMBL; RCBY01000039; RQH46697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6PFJ4; -.
DR   OrthoDB; 9771073at2; -.
DR   UniPathway; UPA00796; UER00771.
DR   Proteomes; UP000269154; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0033320; P:UDP-D-xylose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00081; Hint; 2.
DR   Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR044516; UXS.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
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; 2.
DR   Pfam; PF14890; Intein_splicing; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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   Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269154};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          389..516
FT                   /note="DOD-type homing endonuclease"
FT                   /evidence="ECO:0000259|PROSITE:PS50819"
FT   DOMAIN          573..597
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
SQ   SEQUENCE   738 AA;  84416 MW;  FF7B9EE1F43E7A8B CRC64;
     MRILVTGGAG FLGSHLIDRL MEKGHEVICL DNFYTGTKRN ILKWLNHPYF ELVRHDITEP
     IRLEADQIYH LACPASPIHY QYNPVKTIKT NVMGTLNMLG LAKRVKARFF LASTSEVYGD
     PDVHPQTEEY RGNVNCIGIR SCYDEGKRVA ETLAFDYHRQ NNVDIRVVRI FNSLTGDQKV
     LYYIGKELYY ESFAECYDRI NGDISNVSVP CFDENSKTVI KPISAIWKHH VKKKGYQIKT
     VWGKQIKITE DHSLFTRNNN DRPQAAFGNE LKVGDEIGVP NYISFLEQPL QPFYITDKIC
     IQEEIFLESE ETISYIEKYG DKIREYLLAK GVNPEQLYSI LKSYEAKNKI PLHLWEYLEL
     PLSKKEKICY LSSKAIKNWV GNIEEFLWLL GFYVSQGSFI DNELVFKGGA EKLAKLIEVV
     ERIFECQCEI KIEGSISIRS KILVDLIGEG LNFGNKEKEI SNWVLQLPQK QLISFLQGLN
     EGNNVVENQP NLNIEFKSGS QAIAEKLVLI LAKFGLVANV SEIEQNYQII VQGLEDNNIE
     NLSNIQQKIS AKRTGDIVWA KIESIEEFEI DDYVYDFSVP NYENFIGGSY GIFAHNTYGP
     RMLENDGRVV SNFIAQALKG TPLTVYGDGS QTRSFCYVSD LVEGFIRLMD QDFIGPVNIG
     NPGEYTILEL AQTIQQMVNP DAEITYKPLP QDDPKQRQPD ITRAKKYLGW EPSVPLQEGL
     KLTIEDFRER LKNEPPKS
//
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