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Database: UniProt
Entry: A0A0D2D7U5_9EURO
LinkDB: A0A0D2D7U5_9EURO
Original site: A0A0D2D7U5_9EURO 
ID   A0A0D2D7U5_9EURO        Unreviewed;       391 AA.
AC   A0A0D2D7U5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=UDP-glucose/GDP-mannose dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM00984};
GN   ORFNames=PV05_02892 {ECO:0000313|EMBL:KIW58367.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58367.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW58367.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58367.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) 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; KN847318; KIW58367.1; -; Genomic_DNA.
DR   RefSeq; XP_013318951.1; XM_013463497.1.
DR   AlphaFoldDB; A0A0D2D7U5; -.
DR   STRING; 348802.A0A0D2D7U5; -.
DR   GeneID; 25324800; -.
DR   HOGENOM; CLU_023810_0_1_1; -.
DR   OrthoDB; 5399932at2759; -.
DR   Proteomes; UP000054342; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   DOMAIN          297..390
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   391 AA;  42883 MW;  2BA40393A8704CC9 CRC64;
     MVSSTLGKVA IVGVGFVGEA LLREFSHVHH TIGFDISEAR IKDLRTKYAG EKRMTLTTDE
     TALDQAAHFL ISVPTLMKAD HSVDVSYLKS ALSTVFRHAK PGSTIVIEST VSVGTTRQLF
     SSVQQHFNCG MSPERVDPGR TFPAACDIPK IISGLTPQAL EVIEALYSTV FNHVVPVSRP
     EIAEMTKLFE NCYRMINIAY ANEVSDACRT LGLDPHEVID AAATKPYGFQ AFRPGLGVGG
     HCIPVNPSYL LQTCPNLPVL EQSTKIMRER PLKLARELHA HCCSSTLAST DLRPRVLVVG
     VGFKPGQSVL SHSPAIDFAN ELQNSGCDRL AFYDPLVSQE AVPWMEKLED DAFNPSELAA
     DFDVVAVCTR QHGVDFNVLQ HLPTEMVWSY D
//
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