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Database: UniProt
Entry: A0A1G5FY01_9BACL
LinkDB: A0A1G5FY01_9BACL
Original site: A0A1G5FY01_9BACL 
ID   A0A1G5FY01_9BACL        Unreviewed;       631 AA.
AC   A0A1G5FY01;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Nucleotide sugar dehydrogenase {ECO:0000313|EMBL:SCY43987.1};
GN   ORFNames=SAMN05720606_1052 {ECO:0000313|EMBL:SCY43987.1};
OS   Paenibacillus polysaccharolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=582692 {ECO:0000313|EMBL:SCY43987.1, ECO:0000313|Proteomes:UP000198538};
RN   [1] {ECO:0000313|EMBL:SCY43987.1, ECO:0000313|Proteomes:UP000198538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL9 {ECO:0000313|EMBL:SCY43987.1,
RC   ECO:0000313|Proteomes:UP000198538};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMVM01000005; SCY43987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5FY01; -.
DR   STRING; 582692.SAMN05720606_1052; -.
DR   Proteomes; UP000198538; 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: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.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          370..466
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..584
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  69227 MW;  99779C5A796E9768 CRC64;
     MSENSLNPEE KRQDEKEKQA QTPGEHRGRK QQRLKQLYPK PQQTTLQCIH DRSLKAVVIG
     LGYVGLPMAV EMAQSGYQVH GIDIDAGKVA KLRAGHSYII GIEDEMLQTL LEANLLTAGT
     DYAAVAGADV IVICVPTPLT DKHQPDISYI SSAVGGMTPY LQQGSLVILE STTYPGTTEE
     HVKQPIEAAR GWTAGEHFYV CYSPERVDPG SVHYGVKNTP KIIGGSTPAC LSYGTQFYGS
     FLNEVVPVSS TTVAETAKLF ENTFRSVNIA LVNELTPACE QMGVDIWEVL QAAATKPFGY
     MPFYPGPGIG GHCIPIDPIY LSWAANRQGS ELRFIELADA TNRQMPEHVV QRATALLEQR
     GHSIRGARVV LAGMAYKKDI DDLRESPALD VFRLLSAAGA DVVFTDPMVP VFRQDDGSML
     QSRQATPELW TWADLVIITT DHSSFDYQEM ADHAPLIFDT RNATAGCRGN NIVVLGQPER
     HDHGRTLGLE QEKGQGAERE KGVQSEYLKH AGHEEHEKYE EVVEDAELAE TEHVEHEEQG
     MEKEEFQDTE HEASGSKGHS NSGQTTREKD SAGADVKGQN ERYPGTKRES VPSGEGAEKE
     NGESHGIQDD AWADQDMKNV HGKTGDGYGE S
//
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