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Database: UniProt
Entry: A0A1A7KJ01_9FLAO
LinkDB: A0A1A7KJ01_9FLAO
Original site: A0A1A7KJ01_9FLAO 
ID   A0A1A7KJ01_9FLAO        Unreviewed;       427 AA.
AC   A0A1A7KJ01;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=UDP-N-acetyl-D-glucosamine 6-dehydrogenase {ECO:0000313|EMBL:OBW42112.1};
DE            EC=1.1.1.136 {ECO:0000313|EMBL:OBW42112.1};
GN   Name=wbpA_1 {ECO:0000313|EMBL:OBW42112.1};
GN   ORFNames=AB670_01532 {ECO:0000313|EMBL:OBW42112.1};
OS   Chryseobacterium sp. MOF25P.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1664318 {ECO:0000313|EMBL:OBW42112.1, ECO:0000313|Proteomes:UP000092708};
RN   [1] {ECO:0000313|EMBL:OBW42112.1, ECO:0000313|Proteomes:UP000092708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOF25P {ECO:0000313|EMBL:OBW42112.1,
RC   ECO:0000313|Proteomes:UP000092708};
RA   David V.-J., Thomas B., Ramon P.Y., Thao N., David R., Richard E.,
RA   Roderick C., Nikki M., Timothy W.J., Alexander A.E., Kimberley T.;
RT   "A floR containing integrative conjugative element found in multidrug
RT   resistant Chryseobacterium spp. isolates: exception to the general rule?";
RL   Submitted (JUN-2015) 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:OBW42112.1}.
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DR   EMBL; LFEG01000050; OBW42112.1; -; Genomic_DNA.
DR   RefSeq; WP_066677494.1; NZ_LFEG01000050.1.
DR   AlphaFoldDB; A0A1A7KJ01; -.
DR   PATRIC; fig|1664318.4.peg.1573; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000092708; 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:0047004; F:UDP-N-acetylglucosamine 6-dehydrogenase activity; IEA:UniProtKB-EC.
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   ECO:0000313|EMBL:OBW42112.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092708}.
FT   DOMAIN          324..422
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   427 AA;  47323 MW;  6FA5399720FC079F CRC64;
     MNTQHQIAII GLGYVGLPLA RLFATKYNTV GFDINETRIH ELRSGTDNTL EVENEVLQAV
     LVDSPNEEKG LYVTNQLDEI KNCNYFIITV PTPVDKNNRP DLTPLFKASE TVGKVLKKGD
     IIIYESTVYP GATEEDCIPV VEKTSGLKFN VDFFAGYSPE RINPGDKEHT VEKILKVTSG
     STPEIGKKVD DLYKSVITAG THLAPTIKVA EAAKVIENSQ RDINIAFVNE LAKIFNLLNI
     DTHAVLEAAG TKWNFLPFKP GLVGGHCIGV DPYYLAQKAQ EHGYHPEIIL AGRRLNDSMG
     EYVASQVVKT MIKKDIKVNG AKVLNLGITF KENCPDVRNT KAVDVISALE DYSMKVTTFD
     PWANPEEVMH EYNLDCSSEL VEGTKYDAII LTVAHNEFTN LDLNQFLIEG GVVYDVKGIL
     KDCDNRL
//
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