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Database: UniProt
Entry: R4G1C2_9BACI
LinkDB: R4G1C2_9BACI
Original site: R4G1C2_9BACI 
ID   R4G1C2_9BACI            Unreviewed;       423 AA.
AC   R4G1C2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=NDP-N-acetyl-D-galactosaminuronic acid dehydrogenase {ECO:0000313|EMBL:GAC91763.1};
GN   ORFNames=KN10_2199 {ECO:0000313|EMBL:GAC91763.1};
OS   Anoxybacillus flavithermus NBRC 109594.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=1315967 {ECO:0000313|EMBL:GAC91763.1, ECO:0000313|Proteomes:UP000013057};
RN   [1] {ECO:0000313|Proteomes:UP000013057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 109594 {ECO:0000313|Proteomes:UP000013057};
RA   Matsutani M., Shirakihara Y., Imada K., Yakushi T., Matsushita K.;
RT   "Draft Genome Sequence of a Thermophilic Member of the Bacillaceae,
RT   Anoxybacillus flavithermus Strain Kn10, Isolated from the Kan-nawa Hot
RT   Spring in Japan.";
RL   Genome Announc.1:e00311-13(2013).
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:GAC91763.1}.
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DR   EMBL; BARH01000019; GAC91763.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4G1C2; -.
DR   Proteomes; UP000013057; 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; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..423
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038566387"
FT   DOMAIN          315..413
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   423 AA;  47157 MW;  37E3F317BA9A11C8 CRC64;
     MYKMKKVCVI GLGYIGLPTA TVLANNGFEV HGVDINEKAV ELINNGQVHI YEPDLDIMVK
     KAVESGNLKA SVIPEKADVF IIAVPTPFKE NHKPDLTYVE QATRSISPYL EPGNIVILES
     TSPVGTTEKV AEWILEERED LSIDENRENR IFVSHCPERV LPGKILKELI ENNRIIGGIN
     EESTKRTVGF YKSFVKGKIL ETNARTAELS KLAENAFRDV NIAFANELSM ICDELNINVW
     ELINLANHHP RVNILQPGPG VGGHCIAVDP WFIVDAAPET AKLIRTARMV NDSKPYFVIE
     KIKEATKNLK NPTIACLGLA FKANVDDLRE SPAVKIVKEL SAIYDQTIYV AEPHIEELPK
     DLLELNVRLV KTEDAIEKAD VVVLLVDHDY FKVIDKKALL NKIVIDTRGV LPITSNIEVS
     MII
//
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