GenomeNet

Database: UniProt
Entry: A0A0P6X1H6_9CHLR
LinkDB: A0A0P6X1H6_9CHLR
Original site: A0A0P6X1H6_9CHLR 
ID   A0A0P6X1H6_9CHLR        Unreviewed;       440 AA.
AC   A0A0P6X1H6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=ADM99_01485 {ECO:0000313|EMBL:KPL74775.1};
OS   Leptolinea tardivitalis.
OC   Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Leptolinea.
OX   NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL74775.1, ECO:0000313|Proteomes:UP000050430};
RN   [1] {ECO:0000313|EMBL:KPL74775.1, ECO:0000313|Proteomes:UP000050430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL74775.1,
RC   ECO:0000313|Proteomes:UP000050430};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH +
CC         UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885;
CC         EC=1.1.1.22; Evidence={ECO:0000256|PIRNR:PIRNR000124};
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:KPL74775.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LGCK01000002; KPL74775.1; -; Genomic_DNA.
DR   RefSeq; WP_062423194.1; NZ_LGCK01000002.1.
DR   EnsemblBacteria; KPL74775; KPL74775; ADM99_01485.
DR   PATRIC; fig|229920.5.peg.3112; -.
DR   Proteomes; UP000050430; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; 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   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; IPR028357; UDPglc_DH_bac.
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; PIRSF500134; UDPglc_DH_bac; 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:UP000050430};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050430}.
FT   DOMAIN      315    416       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    262    262       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      31     31       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      36     36       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      87     87       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     122    122       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     157    157       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     265    265       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     329    329       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   440 AA;  48315 MW;  C50D10AAB6993B23 CRC64;
     MSKICVIGTG YVGLVTGTCF ADLGNSVTCL DVDETRISKL LKGIMPIYEP GLQEIVERNV
     KAGRLIFTTD YVKAVKDAEI AFIAVGTPSG VDGEADLQYV RQAAESIADL VDSKIIVVNK
     STVPVGTGDW VAEVIQKRRN GRPLDLNVVS NPEFLREGSA INDFMQSDRV VLGSENRTAA
     EKVAELYAPL RCPVLITDLR TAEMIKYASN AFLATRISFI NEIANVCEEL GADVKVVAQG
     MGLDKRIGSA FLDAGLGWGG SCFPKDVKAL AHMAVLHGTH PQLLQAVMEI NRNQRRRLVY
     KLRKALGGLN DRTIGVLGIS FKPNTDDIRE APALEVIHLL ENEGAKIKAY DPQAMENAAQ
     ILQKVKLCDN PYQVAEGSDA LILITEWNEF KQIDFNKIKE LMNQPVIMDG RNLWDEKTLK
     NMGFQYFGVG RATKPTNTLD
//
DBGET integrated database retrieval system