ID A0A0M2U969_9FIRM Unreviewed; 447 AA.
AC A0A0M2U969;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:KKM10836.1};
GN ORFNames=SY88_11565 {ECO:0000313|EMBL:KKM10836.1};
OS Clostridiales bacterium PH28_bin88.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1605376 {ECO:0000313|EMBL:KKM10836.1, ECO:0000313|Proteomes:UP000034222};
RN [1] {ECO:0000313|EMBL:KKM10836.1, ECO:0000313|Proteomes:UP000034222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Robbins S., Tyson G.;
RT "High quality genome sequence of Candidatus Suratobacter aromatica.";
RL Submitted (MAR-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:KKM10836.1}.
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DR EMBL; LAKY01000049; KKM10836.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M2U969; -.
DR STRING; 1605376.SY88_11565; -.
DR PATRIC; fig|1605376.3.peg.2109; -.
DR Proteomes; UP000034222; 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 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000034222}.
FT DOMAIN 338..436
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 447 AA; 49352 MW; 5C76BC44FA3528AB CRC64;
MQATGADHLT AAELKRKIQT HTANVAVVGL GYVGLPLAVE KAKVGFNVLG IEQNPKRAHK
VNNGENYILD VKDEDLQKVV HEGKLKAYTD FACLPEANVT VICVPTPLNT NRDPDISYIV
NVTNEIAKHL RSGQLVTLES TTYPGTTQEV ILPKLEATGL KVGQDFFLAF SPERVDPGNK
RFTTHNTSKV VGGVTLACLD VAYTFYAQTI QHVVPVSSPA VAEMTKVFEN TYRAVNIALV
NELMLLCDKM GIDVWEVVDA AATKPFGIQT FYPGPGVGGH CIPIDPFYLT WKAREYDFHT
RFIELAGEIN VEVSYYVVNK VIRALNQMQK CLHGSKILVL GVAYKKDVAD VRESPALRII
DQLLRHGAEV TYHDPLVPFI EPHGNSTFSA ESVLLAESTL AVADCVLIIT DHSGIDYEWV
VQHSQLVVDT RNATKYVKNN REKIVKI
//
