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Database: UniProt
Entry: A0A0D4BXG7_9MICC
LinkDB: A0A0D4BXG7_9MICC
Original site: A0A0D4BXG7_9MICC 
ID   A0A0D4BXG7_9MICC        Unreviewed;       445 AA.
AC   A0A0D4BXG7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=UM93_03640 {ECO:0000313|EMBL:AJT40830.1};
OS   Psychromicrobium lacuslunae.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Psychromicrobium.
OX   NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT40830.1, ECO:0000313|Proteomes:UP000061839};
RN   [1] {ECO:0000313|EMBL:AJT40830.1, ECO:0000313|Proteomes:UP000061839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT40830.1,
RC   ECO:0000313|Proteomes:UP000061839};
RX   PubMed=25908143;
RA   Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter
RT   sp. Strain IHBB 11108 Using PacBio Single-Molecule Real-Time
RT   Sequencing Technology.";
RL   Genome Announc. 3:0-0(2015).
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; CP011005; AJT40830.1; -; Genomic_DNA.
DR   RefSeq; WP_045073713.1; NZ_CP011005.1.
DR   EnsemblBacteria; AJT40830; AJT40830; UM93_03640.
DR   KEGG; ari:UM93_03640; -.
DR   PATRIC; fig|1618207.4.peg.742; -.
DR   KO; K00012; -.
DR   OrthoDB; 647136at2; -.
DR   Proteomes; UP000061839; Chromosome.
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:UP000061839};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061839}.
FT   DOMAIN      318    419       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    262    262       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      85     85       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     121    121       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     265    265       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     332    332       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   445 AA;  46749 MW;  5006A4721EAD1B71 CRC64;
     MKISVIGCGY LGAVHAASLA SFGHQVIGVD HDERKIEHLS RGFAPFFEAG LEPLLKAGLE
     QGRLSFSTDF AALAEAELHF ICVGTPQSKT TQEADLSSLL SVVEGLHPYL RPGTLVVGKS
     TVPVGTAAAI AEAIAGTGAV LAWNPEFLRQ GSAVADSLQP DRLVYGIPKG IGAGRSQHLL
     DQVYAPILAA GVPRLVTDLA TAELTKVAAN AFLALKLSYI NAVGELCEAT GADVTELARA
     LGLDERIGAK YLAAGAGFGG GCLPKDIRSF RAQAAKHGIE PLEELMSLID GINADARYRI
     AEAASQLCSG TLAGKKIAIL GAAFKPNTDD IRDSPALDVA LQLAQQGAEV VVTDPQAVNQ
     AWLQYPQLRF ETQLDAALQG AELVVLMTEW QEYRQLQPAA VASLVARPVL LDGRNALDAA
     SWRAAGWRYR GIGVGSADQL TADIS
//
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