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Database: UniProt
Entry: A0A2S4XIC0_9ACTN
LinkDB: A0A2S4XIC0_9ACTN
Original site: A0A2S4XIC0_9ACTN 
ID   A0A2S4XIC0_9ACTN        Unreviewed;       298 AA.
AC   A0A2S4XIC0;
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=UDP-glucose 6-dehydrogenase {ECO:0000313|EMBL:POX36341.1};
GN   ORFNames=C3486_34140 {ECO:0000313|EMBL:POX36341.1};
OS   Streptomyces sp. Ru73.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX36341.1, ECO:0000313|Proteomes:UP000236956};
RN   [1] {ECO:0000313|EMBL:POX36341.1, ECO:0000313|Proteomes:UP000236956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru73 {ECO:0000313|EMBL:POX36341.1,
RC   ECO:0000313|Proteomes:UP000236956};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00006601, 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:POX36341.1}.
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DR   EMBL; PQSQ01000139; POX36341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4XIC0; -.
DR   OrthoDB; 5193947at2; -.
DR   Proteomes; UP000236956; 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; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013332; KPR_N.
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   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   PANTHER; PTHR43750:SF3; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   Pfam; PF02558; ApbA; 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; 2.
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:UP000236956}.
FT   DOMAIN          4..51
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          60..170
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03721"
FT   DOMAIN          186..280
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF00984"
SQ   SEQUENCE   298 AA;  32019 MW;  58ACDDB37FEB66E4 CRC64;
     MARIFIVGSG VVGTATGKGF LHAGHEVTFI DISRQRLEYL RSQGLDARDV LDLRNEPDGF
     IFLTLPTPNV GHRYDLSAFE DGTASVGAAL AEATGDHTVV VRSTVPPGTT EGLVQTLLEK
     HSGKTVGEGF ALAGNPEFLR AATALEDFRH PWMTVIASRS QRTVERLTEL LAPFGGELRT
     FSNPAAAELV KCAHNIFNAT KISFWNEMWL VAQTLGLDLD PIAQTVARSA EGSYNPLYGI
     RGGAPYGGVC LPKDTQGFLG LAESLSLDMP LLKAVVKVND TLIERADREA DELAAELA
//
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