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Database: UniProt
Entry: A0A2V2Q328_9ACTN
LinkDB: A0A2V2Q328_9ACTN
Original site: A0A2V2Q328_9ACTN 
ID   A0A2V2Q328_9ACTN        Unreviewed;       420 AA.
AC   A0A2V2Q328;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:PWS42023.1};
GN   ORFNames=DKT74_24370 {ECO:0000313|EMBL:PWS42023.1};
OS   Streptomyces sp. ZEA17I.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS42023.1, ECO:0000313|Proteomes:UP000245984};
RN   [1] {ECO:0000313|EMBL:PWS42023.1, ECO:0000313|Proteomes:UP000245984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZEA17I {ECO:0000313|EMBL:PWS42023.1,
RC   ECO:0000313|Proteomes:UP000245984};
RA   Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT   "Genome sequencing and identification of chitinase family genes of
RT   Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
RL   Submitted (MAY-2018) 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:PWS42023.1}.
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DR   EMBL; QGMS01001340; PWS42023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V2Q328; -.
DR   Proteomes; UP000245984; 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; IPR029752; D-isomer_DH_CS1.
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:SF1; 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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          319..414
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   420 AA;  44777 MW;  C276BBCBF1EF29A0 CRC64;
     MPADLAVIGL GHLGLPLVQA AVAAGIDTVG YDTDPRPCAE LRAGRTPVEG SLTASEIRRM
     LSGGFRPTTS AAELGRVRTA VICSPTPLGP DRTVDLTALR DAARALAARL RPHTTVLLES
     AVPPGTTENV LRPLLEEGSG LVAGRDFHLA CSPSRLDPGN RTHTYASTPK VIGGLTPACT
     ESAAAFYGRL TDKVVRARGP REAEMTKVLE TNFRHVNIAL VNEMAVACHD LGVDLWDVIR
     CAETKPFGFH PFRPGPGVGG HGVPVDPGSL PYSGRTPGHP LRMVSLAQEI NERMPSYVIQ
     RCATLLNEHG KSVRGARVLL LGVTYKPDSA DQEAAPAREI AGRLMDMGAQ IGYHDPHVLD
     WRVRQLPVPR ADSLYEAAAA ADLTVLLQQH RTYDLQGLAV KAQLLLDTRG ATPAGAAHRL
//
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