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Database: UniProt
Entry: A0A257LX58_9BACT
LinkDB: A0A257LX58_9BACT
Original site: A0A257LX58_9BACT 
ID   A0A257LX58_9BACT        Unreviewed;       434 AA.
AC   A0A257LX58;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   10-APR-2019, entry version 8.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=CGW93_00485 {ECO:0000313|EMBL:OYV03546.1};
OS   candidate division bacterium WOR-3 4484_18.
OC   Bacteria; candidate division WOR-3.
OX   NCBI_TaxID=2020626 {ECO:0000313|EMBL:OYV03546.1};
RN   [1] {ECO:0000313|EMBL:OYV03546.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4484_18 {ECO:0000313|EMBL:OYV03546.1};
RX   PubMed=28835260; DOI=10.1186/s40168-017-0322-2;
RA   Dombrowski N., Seitz K.W., Teske A.P., Baker B.J.;
RT   "Genomic insights into potential interdependencies in microbial
RT   hydrocarbon and nutrient cycling in hydrothermal sediments.";
RL   Microbiome 5:106-106(2017).
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:OYV03546.1}.
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DR   EMBL; NMUJ01000003; OYV03546.1; -; Genomic_DNA.
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   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      319    419       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    265    265       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      37     37       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      42     42       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      91     91       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     126    126       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     160    160       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     268    268       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     333    333       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   434 AA;  47790 MW;  B43D3C4A2241BF32 CRC64;
     MNHSHTSQTL CVIGLGYVGL TTVVGFAELG HKVIGVDVDD EKIKTLNCGI SPIYEVGMEQ
     LLRKNRDRLT FTVDLKEAVT SSSIIFVAVG TPTKDTGEAD LSQIINVAHG LSESINNYKI
     IVIKSTVPVG SVDLIRNILS QKCKEGKDFD LVVNPEFLRE GNAIHDFFNP SRVVIGADNK
     QAAQVVAQLY KPLSTPVLLT SPIDAQMIKY AANAFLASRI SFINEIATIS ERVGADIKNI
     IKGLSYDPRL GDGYLSPGIG FGGPCLTKDL KALIHMAQSY DYEPRFLKSI FERNEEQIQS
     IVWKVKKALG GILYGKTVGV LGLSFKPCTK DIRNSPAVRI VKLLKQGGAF IKAYDPMAID
     EAKTILPDIE YCATPYEFKN LDLLLLLVGW EEFKQLDYRR LKKGMSTPII IDGVNLLEPE
     VMKKLGFTYS GIGR
//
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