ID C5LUX2_PERM5 Unreviewed; 943 AA.
AC C5LUX2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|ARBA:ARBA00012954};
DE EC=1.1.1.22 {ECO:0000256|ARBA:ARBA00012954};
GN ORFNames=Pmar_PMAR025860 {ECO:0000313|EMBL:EEQ99472.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EEQ99472.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate
CC biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004701}.
CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00006601}.
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DR EMBL; GG685688; EEQ99472.1; -; Genomic_DNA.
DR RefSeq; XP_002766755.1; XM_002766709.1.
DR AlphaFoldDB; C5LUX2; -.
DR EnsemblProtists; EEQ99472; EEQ99472; Pmar_PMAR025860.
DR GeneID; 9050880; -.
DR InParanoid; C5LUX2; -.
DR OrthoDB; 167209at2759; -.
DR UniPathway; UPA00038; UER00491.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017476; UDP-Glc/GDP-Man.
DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR InterPro; IPR028356; UDPglc_DH_euk.
DR NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR PANTHER; PTHR11374:SF3; UDP-GLUCOSE 6-DEHYDROGENASE; 1.
DR PANTHER; PTHR11374; UDP-GLUCOSE DEHYDROGENASE/UDP-MANNAC DEHYDROGENASE; 1.
DR Pfam; PF00984; UDPG_MGDP_dh; 1.
DR Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR PIRSF; PIRSF500133; UDPglc_DH_euk; 1.
DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR500133-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 777..905
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
FT REGION 9..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 721
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-1"
FT BINDING 457..462
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 482
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 487
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 535..539
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 576..577
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 610
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 721..724
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
FT BINDING 791
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR500133-3"
SQ SEQUENCE 943 AA; 103829 MW; F7974C50167B3FB4 CRC64;
MTSQFQFHCD ESNRLHLPPQ QHYPRKSGIR RKASQARRHP RSVVLMATDF TPMAKAPQTL
LSFPEVEELS RTVLLTNMPM PPNTTGYDLS PAEMAAVAKF YSNWLTTYGS IEKVELCDPA
GSLVCVFTHR EGALLAVAGM HQSRPVVVGT RGNARDGQVI ATLASNRRKL HTIKGRQIYS
YEGMLPFTTT NGHISDTKVT VVVCLKNLPP ESTREQVYAV ISRFSRSVYI PPEPQIAGKL
LCYFRSSGEA HIFMAAVNYA CGDGPVYLAE ETYRNFIPRS WIVAEVHAHK FRDSQGKNST
SITPLLSTAR NRYSALDVLL RMARGRLDAD SMCSNDDSYM LETSCDGSVR CPPSSARSTP
RSAPLLVPPA AFQDPIGNLL VHNPIAIHAL RRAYEMLADW YPPGALTLAK PEANVRHQKQ
LSSCLWRNHI EEGVHGSAVG QNSPIRNICT TRVCCIGAGY VGGPTMAMIA YKCPHIQVCV
VDLSEERIAA WNSDELPIYE PGLAEIVKEC RGRNLHFSTN VASAVADCDI IFVSVNTPTK
KHGQGAGRAA NLAPWEGAGR TIAAHARGPK IIIEKSTVPV RTAAALQRVL DGQGTSQKYV
ILSNPEFLAE GTAMADLANP DRVLIGGPQN SDGRFAIDVV VGVYASWVPR ERIITTNLWS
SELSKLVANA FLAQRVSSIN AISMLCEKTG ADVNEVAHAI GTDSRIGPKF LSASVGFGGS
CFQKDILNLV YLCEQFNLPE VANYWRQVVE MNDLQKTHFV QTIINSMFNT VQGKKICILG
FAFKKDTGDT RETAALSVCA QLMHDGAILH VYDPQVTREQ VSRRNREFTG ICFHQALLEF
SDHDMSFDFD KQFVSAIDPA SAAKGSHAIV VLTEWDMFKE LPYEEYFNTM IKPAFIFDGR
NILNHGSLIK IGFEVHAIGK ALRNRGLIKA TPRSVTDSPE LGM
//
