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Database: UniProt
Entry: A0A150FSA6_CLOPD
LinkDB: A0A150FSA6_CLOPD
Original site: A0A150FSA6_CLOPD 
ID   A0A150FSA6_CLOPD        Unreviewed;       438 AA.
AC   A0A150FSA6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:KXZ40503.1};
DE            EC=1.1.1.22 {ECO:0000313|EMBL:KXZ40503.1};
GN   ORFNames=JWYL7_1578 {ECO:0000313|EMBL:KXZ40503.1};
OS   [Clostridium] paradoxum JW-YL-7 = DSM 7308.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=1121328 {ECO:0000313|EMBL:KXZ40503.1, ECO:0000313|Proteomes:UP000092605};
RN   [1] {ECO:0000313|EMBL:KXZ40503.1, ECO:0000313|Proteomes:UP000092605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW-YL-7 {ECO:0000313|EMBL:KXZ40503.1,
RC   ECO:0000313|Proteomes:UP000092605};
RA   Utturkar S.M., Lancaster A., Poole F.L., Adams M.W., Brown S.D.;
RT   "Draft genome sequence for Clostridium paradoxum JW-YL-7.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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:KXZ40503.1}.
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DR   EMBL; LSFY01000001; KXZ40503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A150FSA6; -.
DR   STRING; 1121328.JWYL7_1578; -.
DR   PATRIC; fig|1121328.3.peg.1589; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000092605; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
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; IPR028359; UDP_ManNAc/GlcNAc_DH.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43491; UDP-N-ACETYL-D-MANNOSAMINE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43491:SF2; UDP-N-ACETYL-D-MANNOSAMINE 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; PIRSF500136; UDP_ManNAc_DH; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KXZ40503.1}.
FT   DOMAIN          328..423
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   438 AA;  48893 MW;  9DA802109D6F962C CRC64;
     MIKDSLKNVA VFGQGFVGLP LALSFAMRGS NVYGVDVVKV LVEEINEGIT HHTEQFEGKT
     ITQILKEQLK EKRYKATTNA KEALEVCNNI VVTVGIPIRD SKYDFSDLEE CVVTIAKNLK
     KGDLVLIRST VIPGTTEEKL LPILERESGL KAGEDFYLAY SSERIAEGKA FDEFAYMPTI
     VAGINEESTK RAKELLEVVC KTDVIVASNI KVVETSKVFE NVQRDVNIAM VQEFARFTES
     LGIDIYEVIK IANTHKRVNL LIPGPGVGGY CIPNAYHYLA PKAEELNVDL SLLKLAREKN
     RNLPNVMVNM LESMLLKENK TLENAKIGIL GIAMKDYSND DRISPPIEII NILKKRGAIV
     SAYDSAVPTA YDFKVDNIEQ ALKGKDAIMI LAKQESYDDL NEKYIGMIEK GTVILDTRNI
     FEGKEDKLKE YGIKLMKI
//
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