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Database: UniProt
Entry: M7NL49_9BACL
LinkDB: M7NL49_9BACL
Original site: M7NL49_9BACL 
ID   M7NL49_9BACL            Unreviewed;       425 AA.
AC   M7NL49;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=UDP-glucose 6-dehydrogenase ywqF {ECO:0000313|EMBL:EMR07927.1};
DE            EC=1.1.1.22 {ECO:0000313|EMBL:EMR07927.1};
GN   Name=ywqF {ECO:0000313|EMBL:EMR07927.1};
GN   ORFNames=C772_00256 {ECO:0000313|EMBL:EMR07927.1};
OS   Bhargavaea cecembensis DSE10.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX   NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR07927.1, ECO:0000313|Proteomes:UP000011919};
RN   [1] {ECO:0000313|EMBL:EMR07927.1, ECO:0000313|Proteomes:UP000011919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE10 {ECO:0000313|EMBL:EMR07927.1,
RC   ECO:0000313|Proteomes:UP000011919};
RX   PubMed=23766406;
RA   Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT   from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT   Chagos-Laccadive Ridge System in the Indian Ocean.";
RL   Genome Announc. 1:e00346-13(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:EMR07927.1}.
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DR   EMBL; AOFT01000001; EMR07927.1; -; Genomic_DNA.
DR   RefSeq; WP_008296714.1; NZ_AOFT01000001.1.
DR   AlphaFoldDB; M7NL49; -.
DR   STRING; 1235279.C772_00256; -.
DR   PATRIC; fig|1235279.3.peg.267; -.
DR   eggNOG; COG0677; Bacteria.
DR   OrthoDB; 9803238at2; -.
DR   Proteomes; UP000011919; 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:0003979; F:UDP-glucose 6-dehydrogenase activity; IEA:UniProtKB-EC.
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,
KW   ECO:0000313|EMBL:EMR07927.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011919}.
FT   DOMAIN          307..403
FT                   /note="UDP-glucose/GDP-mannose dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00984"
SQ   SEQUENCE   425 AA;  47212 MW;  9DA18D74374294B6 CRC64;
     MTKNLCVIGL GYIGLPTAVM FANHGVRVHG VDVNQRAVEM ISNKQLHIEE NGLQERLNNA
     IDSGMLTVST EPVEADAFIV AVPSPIREDR TADLEYVRKA TASIVPYLKK GNLIILESTV
     PPKTVEDVML PELEKSGFAI GEELFVSHSP ERVIPGRIFE ELEQNGRIIG GINEKSAEMT
     KELYEAFVKG PIELTDATTA ELVKVMENTY RDVNIAFANE MAKIGEHLDV NIWDAIRFAN
     FHPRVNIHQP GPGVGGHCIA VDPWFLVELA PEQSNIIHLS RKTNDGMPQF VADRVMELVG
     DSERKIAVLG LSFKADVDDM RQSPSIDVIN HLQEKGFTVA SFDPHVNEGS HPTQVNSVEE
     AAKDAVMILV LTNHMEFKNL QPNQVADSMD EKIIYDTKNC IDLPVWKEAG FRTYLLGDHK
     DNTNE
//
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