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Database: UniProt
Entry: A0A1F6KM20_9BACT
LinkDB: A0A1F6KM20_9BACT
Original site: A0A1F6KM20_9BACT 
ID   A0A1F6KM20_9BACT        Unreviewed;       415 AA.
AC   A0A1F6KM20;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=UDP-glucose/GDP-mannose dehydrogenase C-terminal domain-containing protein {ECO:0000259|SMART:SM00984};
GN   ORFNames=A3A51_01435 {ECO:0000313|EMBL:OGH48141.1};
OS   Candidatus Levybacteria bacterium RIFCSPLOWO2_01_FULL_39_10.
OC   Bacteria; Candidatus Levybacteria.
OX   NCBI_TaxID=1798622 {ECO:0000313|EMBL:OGH48141.1, ECO:0000313|Proteomes:UP000178689};
RN   [1] {ECO:0000313|EMBL:OGH48141.1, ECO:0000313|Proteomes:UP000178689}
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:OGH48141.1}.
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DR   EMBL; MFOV01000004; OGH48141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6KM20; -.
DR   STRING; 1798622.A3A51_01435; -.
DR   Proteomes; UP000178689; 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: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}.
FT   DOMAIN          315..406
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   415 AA;  45968 MW;  C32A0F9E5041AF1F CRC64;
     MDYSKVLFEK IRRRRARVGI IGIGYVGDAL GKGARGAGFD VLGLTRDPEK AKRINSDKSF
     GYSATSNIED LKRCDIVCIC VPTPIKNDKT PDLDPLVSSL AKTSKILTPA TLVIIESTVA
     AGTTRNIVLP ILKMSGLSEE KDFYLSFSPE RVDPGNLNYG INNTPKVVSG LSITSKNLTH
     LFYSSFIESV VSVSSLETAE MSKLLENAYR FINISFMNEL LDYANSLGVN LWEVIEAASS
     KPFGFMPHYP GPGIGGHCIP VDPYYLLDDA KKRGIELGIL ERAGFVNDLQ PRKVVEKTIE
     VLKKTNGVKN SHSALLVGIS YKEDTPDNRE SPSLIIWSLL KENKIKVDYH DPYFPAYNGA
     RSIDLSSPTI NKKDIIVLTT PHSTIDYERI ISLGKPIIDT KNALKNYSYP HIYRI
//
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