ID A0A1G0W9M0_9BACT Unreviewed; 435 AA.
AC A0A1G0W9M0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:OGV17975.1};
GN ORFNames=A2X47_07695 {ECO:0000313|EMBL:OGV17975.1};
OS Lentisphaerae bacterium GWF2_38_69.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798570 {ECO:0000313|EMBL:OGV17975.1, ECO:0000313|Proteomes:UP000176746};
RN [1] {ECO:0000313|EMBL:OGV17975.1, ECO:0000313|Proteomes:UP000176746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV17975.1}.
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DR EMBL; MHBE01000055; OGV17975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0W9M0; -.
DR STRING; 1798570.A2X47_07695; -.
DR Proteomes; UP000176746; 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}.
FT DOMAIN 329..428
FT /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00984"
SQ SEQUENCE 435 AA; 48873 MW; C7227C65005E1DAE CRC64;
MLAKFLEKIE TKEAVIGVLG LGYVGLPLLI EFSKAGFRVV GFDIDPEKGR ILNEGRSYIK
HIQSNNIKKM LDTGKFKFYS DFSHASECDA VILCVPTPLT KQREPDMTYI VDSAEALVPY
VRKDQLYCLE STTYPGTTDE ILKPILEKSG LKAGIDFFLA FSPEREDPNN KDFSTSTIPK
VVGGYNNSSL KAAQAMFNTV ICKTVPVSST AAAEATKLME NIFRCINIAM VNELKIIFDK
MGIDIWEVIN AAKTKPFGYM PFYPGPGLGG HCIPIDPFYL TWKAREFDYP TKFIELAGEI
NSAMPRYVVE KTLNALNDRK KTLNGSKVLI IGLAYKKNVD DIRESPSFKL WELLETKGAT
VDYYDPYCPE VRDTRHYPQY ANKKSLTDLN NISDFEAVII STDHDCIDFN FISKNSRLII
DTRNVLAAND NVIKA
//
