ID A0A2U1JU75_9BACI Unreviewed; 446 AA.
AC A0A2U1JU75;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:PWA08403.1};
GN ORFNames=DCC39_15075 {ECO:0000313|EMBL:PWA08403.1};
OS Pueribacillus theae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pueribacillus.
OX NCBI_TaxID=2171751 {ECO:0000313|EMBL:PWA08403.1, ECO:0000313|Proteomes:UP000245998};
RN [1] {ECO:0000313|EMBL:PWA08403.1, ECO:0000313|Proteomes:UP000245998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T8 {ECO:0000313|EMBL:PWA08403.1,
RC ECO:0000313|Proteomes:UP000245998};
RA Niu L.;
RT "Camelliibacillus theae gen. nov., sp. nov., isolated from Pu'er tea.";
RL Submitted (APR-2018) 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:PWA08403.1}.
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DR EMBL; QCZG01000038; PWA08403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1JU75; -.
DR OrthoDB; 9803238at2; -.
DR Proteomes; UP000245998; 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:UP000245998}.
FT DOMAIN 340..436
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 446 AA; 49769 MW; D65B2741C789CBBD CRC64;
MKTSEIADNL FVKKLMDRLN HKTAVIGVVG LGYVGLPLAV EKAKAGYRVI GFDIQEERVR
KVNEGINYIG DVVDEDLAEI VKHQRLKATT DYSFIREVDA VAICVPTPLD MYKQPNTSYV
ENSANEIAAH LQKGMLVVLE STTYPGTTEE LLKPILEKSG LTCGVDFFLA YSPERVDPGN
KQFNTKNTPK VVGGVTENCT QVAAAMYENV LEGKVHRVSS PAVGEMEKVL ENTFRNINIA
LVNEMAILCN KMGIDVWEVI DAAATKPYGF MPFYPGPGLG GHCIPIDPWY LTWKAREYSY
HTKLIEIAGE INNDMPDYVI KRVMEILNKD GKALNGSHIL ILGVAYKKDI DDCRESPVFP
ILDKLDNGGA KWTVVDPHIN EFSFKDRKVF PEPAITADML ERADLVLIAT NHTAFDYKEI
ALHAKAVFDT RNSSEELCIN PNYYKL
//
