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Database: UniProt
Entry: A0A2N7QU88_9GAMM
LinkDB: A0A2N7QU88_9GAMM
Original site: A0A2N7QU88_9GAMM 
ID   A0A2N7QU88_9GAMM        Unreviewed;       425 AA.
AC   A0A2N7QU88;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=UDP-N-acetyl-D-glucosamine 6-dehydrogenase {ECO:0000313|EMBL:PMQ05222.1};
DE            EC=1.1.1.136 {ECO:0000313|EMBL:PMQ05222.1};
GN   Name=wbpA {ECO:0000313|EMBL:PMQ05222.1};
GN   ORFNames=DyAD56_10235 {ECO:0000313|EMBL:PMQ05222.1};
OS   Dyella sp. AD56.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ05222.1, ECO:0000313|Proteomes:UP000235676};
RN   [1] {ECO:0000313|EMBL:PMQ05222.1, ECO:0000313|Proteomes:UP000235676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD56 {ECO:0000313|EMBL:PMQ05222.1,
RC   ECO:0000313|Proteomes:UP000235676};
RA   Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA   Garbeva P.;
RT   "Bacterial performance in fungal presence.";
RL   Submitted (AUG-2017) 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:PMQ05222.1}.
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DR   EMBL; NRDP01000012; PMQ05222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7QU88; -.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000235676; 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:PMQ05222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235676}.
FT   DOMAIN          318..418
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   425 AA;  46721 MW;  6086D9AF7B36D333 CRC64;
     MQNLEDTKLA IIGLGYVGLP LAVEFGKHYD TVGFDINQRR IDELSSGIDH TLEVNNEELA
     EAKRLRFASQ LSELADRNVY IVTVPTPIDS AKRPDLTPLI RASETLAKVL KRGDTVVYES
     TVYPGCTEEV CVPLLEKGSG LVFNRDFFAG YSPERINPGD KQHRVTSILK VTSGSTPEAA
     DFVDRLYGSI ITAGTHRASS LKVAEAAKVI ENTQRDLNIA LVNDLSILFN KLGIDTLEVL
     QAAGTKWNFL PFRPGLVGGH CISVDPYYLT HKAQEVGHHP DVILAGRRTN DGMGPYVASE
     VIRLMVRKGI NPVRARVLIL GLAFKENCPD LRNTRVVDIV QALRGYNAQV DVHDPWVNAA
     EAEHEYALTP IETPSHGDYD AVIIAVGHRQ FTAWGAEGIR AFGKGSSVIY DVKYVLPREA
     VDGRL
//
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