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Database: UniProt
Entry: A0A1B7LKN9_9FIRM
LinkDB: A0A1B7LKN9_9FIRM
Original site: A0A1B7LKN9_9FIRM 
ID   A0A1B7LKN9_9FIRM        Unreviewed;       456 AA.
AC   A0A1B7LKN9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   13-FEB-2019, 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=A6M21_02155 {ECO:0000313|EMBL:OAT87110.1};
OS   Desulfotomaculum copahuensis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1838280 {ECO:0000313|EMBL:OAT87110.1, ECO:0000313|Proteomes:UP000078532};
RN   [1] {ECO:0000313|EMBL:OAT87110.1, ECO:0000313|Proteomes:UP000078532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMa1 {ECO:0000313|EMBL:OAT87110.1,
RC   ECO:0000313|Proteomes:UP000078532};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) 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:OAT87110.1}.
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DR   EMBL; LYVF01000002; OAT87110.1; -; Genomic_DNA.
DR   RefSeq; WP_066665877.1; NZ_LYVF01000002.1.
DR   EnsemblBacteria; OAT87110; OAT87110; A6M21_02155.
DR   BioCyc; GCF_001655685:A6M21_RS00535-MONOMER; -.
DR   Proteomes; UP000078532; 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:UP000078532};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078532}.
FT   DOMAIN      310    413       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    257    257       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      35     35       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      85     85       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     120    120       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     152    152       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     260    260       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     324    324       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   456 AA;  49175 MW;  840BD80FDE6DD805 CRC64;
     MRIAVIGAGY VGLVAAACLS RSGHEVVCIE KDEGKLAELQ DGRLPFYEAG LAEIFTAGVG
     KGSLHFSSEV AACLDAEVVM IAVGTPARPD GRIDLSQIYG AVSRIVEQAR FPQLIVMKST
     VPPGFGENLK ARLLSRAGVP LTYLANPEFL REGSAVRDWY YPDRIVIGGD QELAVAKLAR
     LYADIDAPVV TMDVGSAEMV KYAANAFLAT KISFINEIAN LCELVGADIL PVARAVGMDR
     RIGGEFLQAG LGYGGSCFPK DTCGLDFVST CNGYAFNLLK AVIEVNNRQR VLALRKLRGM
     LGTLHDKTVC VLGLAFKPGT DDIRESPALD IINLLLDEGV KIRVYDPLAM KNAQRLLPPE
     VYSASGTMAA LEGCHALLVA TAWPEFTGLD WTAVKELMRP PRLVLDGRNC LPAEEIIKNG
     LVYQGVGRPA KPENQPGNII LPKSDRTPFR CQVTRC
//
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