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Database: UniProt
Entry: A0A0A1VLP0_9BURK
LinkDB: A0A0A1VLP0_9BURK
Original site: A0A0A1VLP0_9BURK 
ID   A0A0A1VLP0_9BURK        Unreviewed;       458 AA.
AC   A0A0A1VLP0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   10-APR-2019, entry version 17.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=AVS7_04116 {ECO:0000313|EMBL:GAD24356.1};
OS   Acidovorax sp. MR-S7.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD24356.1, ECO:0000313|Proteomes:UP000030646};
RN   [1] {ECO:0000313|EMBL:GAD24356.1, ECO:0000313|Proteomes:UP000030646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-S7 {ECO:0000313|EMBL:GAD24356.1,
RC   ECO:0000313|Proteomes:UP000030646};
RA   Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT   "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant
RT   Bacterium Acidovorax sp. Strain MR-S7.";
RL   Genome Announc. 1:e00412-13(2013).
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}.
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DR   EMBL; DF238983; GAD24356.1; -; Genomic_DNA.
DR   RefSeq; WP_020229857.1; NZ_DF238983.1.
DR   STRING; 1268622.AVS7_04116; -.
DR   EnsemblBacteria; GAD24356; GAD24356; AVS7_04116.
DR   Proteomes; UP000030646; 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:UP000030646};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030646}.
FT   DOMAIN      332    441       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    278    278       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     164    164       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     281    281       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     346    346       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   458 AA;  49517 MW;  22A3A0B243C07ACB CRC64;
     MKITIAGAGY VGLVSAACFA ELGNHVVCVD RDEGRVARLR QADLPLYEPG LRELVAKNLE
     AGRLAFTTDL PRGVRHGELL FIAVGTPAQA DGAADVGQVL EVARAVGGHL TRFQVIADKS
     TVPVGTAGRV RETIARELAR RVRAGQLRKA PEFAVVSNPE FLKEGAAVDD FMRPDRVVLG
     VPQNAAGRRA EALLRRAYAP FNRNRNRERI VAMDVQSAEL TKYAANALLA TKISFMNDMA
     ALAESLGADI EQVRRGIGSD RRIGYDFIYA GLGYGGSCFP KDVDALCHAA RAAGQRMRVV
     EAVRAVNAAQ PDRFMDKVLR HFGGSLQGRV IALWGLTFKP GTDDVREAPS RRIVRRLAAA
     GAQVRAHDPL VQSLAQLLPG ERPGRLARQV AFCADPLEAA RGADALLIAT EWKVYRSPDL
     AALRRALRAP VVFDGRNLFD PAEMRRAGFS YQGVGRGG
//
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