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Database: UniProt
Entry: A0A0A3HY82_9BACI
LinkDB: A0A0A3HY82_9BACI
Original site: A0A0A3HY82_9BACI 
ID   A0A0A3HY82_9BACI        Unreviewed;       435 AA.
AC   A0A0A3HY82;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   10-APR-2019, entry version 15.
DE   SubName: Full=UDP-N-acetyl-D-glucosamine dehydrogenase {ECO:0000313|EMBL:KGR76195.1};
GN   ORFNames=CD29_17050 {ECO:0000313|EMBL:KGR76195.1};
OS   Lysinibacillus manganicus DSM 26584.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1384049 {ECO:0000313|EMBL:KGR76195.1, ECO:0000313|Proteomes:UP000030416};
RN   [1] {ECO:0000313|EMBL:KGR76195.1, ECO:0000313|Proteomes:UP000030416}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26584 {ECO:0000313|EMBL:KGR76195.1,
RC   ECO:0000313|Proteomes:UP000030416};
RA   Zhang F., Wang G., Zhang L.;
RT   "Draft genome sequence of Lysinibacillus manganicus DSM 26584T.";
RL   Submitted (FEB-2014) 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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KGR76195.1}.
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DR   EMBL; JPVN01000027; KGR76195.1; -; Genomic_DNA.
DR   STRING; 1384049.CD29_17050; -.
DR   EnsemblBacteria; KGR76195; KGR76195; CD29_17050.
DR   Proteomes; UP000030416; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   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; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52413; SSF52413; 1.
DR   TIGRFAMs; TIGR03026; NDP-sugDHase; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030416};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030416};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     29       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      329    425       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
SQ   SEQUENCE   435 AA;  48335 MW;  250C1A60B7E70876 CRC64;
     MVTLKEKLIN KTAVLGVIGL GYVGLPLAVE KAKAGYQTIG FDIQESKVNM VNAGLNYIGD
     VVNEDLKDIV NSGYLKATTD FAQVAKADCV CICVPTPLDK NKQPDISFVK NSAQNIVPYM
     HKEMLIVLES TTYPGTTEEL LKPILETSGL ICGVDFYLAF SPERVDPGNL LYKTKNTPKV
     VGGITEKCTD IASTLYESIL EAPIHKVSSP AIAEMEKILE NTYRNVNIGL VNELSILCNK
     MGINFWEVVD AAKSKPYGFQ AFYPGPGIGG HCIPLDPYYL SWKAKEFGFH TSMIEASMMI
     NDRMPEYCVE RASRILNKWK KAINGSTILV LGIAYKQDID DYRESPALRV IDELEKEGAI
     VRFFDPFVPM YQHQGIIKSG EPALTDELIR NADLVIITTN HSTVNYSFVH QHAKVVFDTK
     NAMKEIESRG KIELL
//
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