ID   M3DDK2_SPHMS            Unreviewed;       420 AA.
AC   M3DDK2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:EMF15894.1};
GN   ORFNames=SEPMUDRAFT_61226 {ECO:0000313|EMBL:EMF15894.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF15894.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF15894.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF15894.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; KB456261; EMF15894.1; -; Genomic_DNA.
DR   RefSeq; XP_016764015.1; XM_016909555.1.
DR   AlphaFoldDB; M3DDK2; -.
DR   STRING; 692275.M3DDK2; -.
DR   GeneID; 27906692; -.
DR   eggNOG; KOG2666; Eukaryota.
DR   HOGENOM; CLU_023810_0_1_1; -.
DR   OMA; IDPWFIV; -.
DR   OrthoDB; 5399932at2759; -.
DR   Proteomes; UP000016931; 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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; 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; PF03721; UDPG_MGDP_dh_N; 1.
DR   PIRSF; PIRSF500136; UDP_ManNAc_DH; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931}.
FT   DOMAIN          22..176
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03721"
FT   DOMAIN          196..270
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00984"
SQ   SEQUENCE   420 AA;  45905 MW;  7886A6C5FFAB25F1 CRC64;
     MTSDTARIKA TLAQERQFHP VVAVVGVGYV GSHLVEAFAR VYEVIAFDVS KQRIEKIAQQ
     FSGSAAVRTT SHAPDLAAAN AILISVPTPL NHDKTIDTTF LEIAIRTIAQ HVRPGVTVVV
     ESTVAIGMTR ELLSFLVATK HAKVGMSPER VDPGRKFPAF QSIPKIISGI DSPSLAAVHQ
     LYGRVFDHLI PVSSLEAAEM TKLYENCQRM VCAAYANEMA DACASLGIDE WEVSRAAASK
     PFGYQPFWPG PGVGGPCIPV NPYYLLKTCN MPILQHATET SWRRPSEIVD RLMRVLENKR
     GTTGARRPLS NLKMRVLVVG VGFKRGQSML HNSPGVAAIQ FLLGKYDLDV EFADPLVDQT
     ALAYVPKLNT SVDWNKNSLE EFAGILVTVD QVGLDMHLLD LLEGVIVHNY SPRSYTLASL
//