ID   W9HRK3_FUSOX            Unreviewed;       460 AA.
AC   W9HRK3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=UDP-glucose/GDP-mannose dehydrogenase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOYG_12496 {ECO:0000313|EMBL:EWY85258.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY85258.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY85258.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; JH717846; EWY85258.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9HRK3; -.
DR   HOGENOM; CLU_023810_0_1_1; -.
DR   OrthoDB; 5399932at2759; -.
DR   Proteomes; UP000030753; 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; 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; 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.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030753}.
FT   DOMAIN          77..227
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03721"
FT   DOMAIN          254..327
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00984"
SQ   SEQUENCE   460 AA;  50782 MW;  4D2C547E1999C9AE CRC64;
     MAQVMPPKPM ANLPALVEKE ILPLIPPGDS SPWKRLDNSF TFYPESPPLS SPSSDTDDLD
     QSLCQSVEVS QNDEPVIAVI GVGYVGTHLV SSFSSKYQVI GFDVSAKRIK DLGLEYQEHE
     NVYLSRDSQD LRRATHFLIS VPTLLRPDKT IDSSYLRDAL KTVGEVARSG STVVIESSVA
     IGMTRQLLGP LAANRQFFAG MSPERVDPGR VEPPVQSIPK IISGLDDITP GSLDAINRVY
     STVFETVIPV SKPEVAEMMK LYENCQRMVC IAYANEMADA CIPHGINPYE VCEAASTKPF
     GYMPYSPGVG VGGHCIPVNP FYLLSNSHFP LLQYATLAMH SRPSRLAERM LKRLRQRVTV
     RTPRVLVAGM GFKAGQSQID NSPGADLVKS LAVSREVDVC WADSLVKQSA LPQVRRLLDE
     DWRKDVLRKF DIIVVASRQA GTSFDILDEL DGVEIERWCQ
//