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Database: UniProt
Entry: A0A2T4C206_TRILO
LinkDB: A0A2T4C206_TRILO
Original site: A0A2T4C206_TRILO 
ID   A0A2T4C206_TRILO        Unreviewed;       451 AA.
AC   A0A2T4C206;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:PTB75554.1};
GN   ORFNames=M440DRAFT_1431268 {ECO:0000313|EMBL:PTB75554.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB75554.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB75554.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB75554.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) 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; KZ679133; PTB75554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4C206; -.
DR   STRING; 983965.A0A2T4C206; -.
DR   Proteomes; UP000240760; 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:UP000240760}.
FT   DOMAIN          64..218
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03721"
FT   DOMAIN          241..315
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00984"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  48788 MW;  697455E8B0B183AF CRC64;
     MDPAQLPLPP SEAGRTPTSS PEPVAPPGQR KEWTYYDVTP PEVSPEEAGT PNSSPGDIHP
     SPYVAVIGVG YVGEHLVDVF SRRYAVIGFD VSEQRIKTLG PKYARIKQVK LTANQSRLKH
     ATHFLISVPT LLLPDKTVDT SYLRSALDIV AKYAARGSTV VFESSVAVGM TRELLGPLAK
     KYGWFAGMSP ERVDPGRTEP AAHQIPKIIS GLDDVVAGSL AAIHQLYGPA FNIVVPVSMP
     EVAELTKLFE NCQRMICIGF VNEMANACKP FGIDPYEVCA AAATKPFGYM PYTPGLGVGG
     HCIPVNPYYL LSTSEFPLLK AATEAMYARP AQIGQSIIDS LCAGRDASAG QPRVLVVGMG
     FKRGQSHLVN SPGLELAKSL VLSEKVAVSF ADPLVTQEAV PQIARLDEVN WTVEFLEQNF
     DMIVVAFKQD GLDFDVLDKL NDSVKVQMWC A
//
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