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Database: UniProt
Entry: A0A1V4QNX0_9DELT
LinkDB: A0A1V4QNX0_9DELT
Original site: A0A1V4QNX0_9DELT 
ID   A0A1V4QNX0_9DELT        Unreviewed;       444 AA.
AC   A0A1V4QNX0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   10-APR-2019, entry version 10.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=BZ151_02500 {ECO:0000313|EMBL:OPX20691.1};
OS   Desulfobacca sp. 4484_104.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Desulfobacca.
OX   NCBI_TaxID=1940691 {ECO:0000313|EMBL:OPX20691.1, ECO:0000313|Proteomes:UP000191519};
RN   [1] {ECO:0000313|Proteomes:UP000191519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic
RT   interdependencies in hydrothermal sediment communities.";
RL   Submitted (JAN-2017) 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:OPX20691.1}.
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DR   EMBL; MUKC01000011; OPX20691.1; -; Genomic_DNA.
DR   Proteomes; UP000191519; 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:UP000191519};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      320    424       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    266    266       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      30     30       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      35     35       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      86     86       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     121    121       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     158    158       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     269    269       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     334    334       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   444 AA;  50099 MW;  D2A462BB80A4A95A CRC64;
     MRIAVIGTGY VGLVTGACFA EMGNDVICVD IDQTKIDLLQ QGQIPIYEPG LEEMVRRNCQ
     EQRLYFTTDM LQAVEKSLFC FIAVGTPQDK DGSADLCFVL EVARDIGRYL NGYKVIVEKS
     TVPVGTALKV QQAIKEELSK RGVEHEFDVV SNPEFLKEGT AIDDFMKPDR IVVGCDNVRT
     AELMKELYGP FVRTHHPIIL MDVVSAELTK YAANAFLATK ISFINEIANI CQKVGANVTD
     IRRGIGSDQR IGNQFLFPGL GYGGSCFPKD MQALIKTAQN HNYQPRILEA VEAVNQDQRR
     IFIEQVLDYF QRDLKGKTLA CWGLSFKPLT DDMREAPSLT VISRLIEHQA HIQAYDPKAM
     PFAKQILGEN QAIFFAESAY QALEGVDGLM IVTEWMMFRE PDFERMRGLM RAPVIFDGRN
     LYDPDKMRKK GFTYFSVGRE KVFS
//
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