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Database: UniProt
Entry: E6STQ2_BACT6
LinkDB: E6STQ2_BACT6
Original site: E6STQ2_BACT6 
ID   E6STQ2_BACT6            Unreviewed;       437 AA.
AC   E6STQ2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 43.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   OrderedLocusNames=Bache_2331 {ECO:0000313|EMBL:ADV44299.1};
OS   Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / P
OS   36-108).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV44299.1, ECO:0000313|Proteomes:UP000008630};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P 36-108;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Bacteroides helcogenes P 36-108.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV44299.1, ECO:0000313|Proteomes:UP000008630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / P 36-108
RC   {ECO:0000313|Proteomes:UP000008630};
RX   PubMed=21475586;
RA   Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Brambilla E., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lucas S.;
RT   "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT   108).";
RL   Stand. Genomic Sci. 4:45-53(2011).
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; CP002352; ADV44299.1; -; Genomic_DNA.
DR   RefSeq; WP_013547889.1; NC_014933.1.
DR   STRING; 693979.Bache_2331; -.
DR   EnsemblBacteria; ADV44299; ADV44299; Bache_2331.
DR   KEGG; bhl:Bache_2331; -.
DR   PATRIC; fig|693979.3.peg.2444; -.
DR   eggNOG; ENOG4105C6Y; Bacteria.
DR   eggNOG; COG1004; LUCA.
DR   HOGENOM; HOG000153773; -.
DR   KO; K00012; -.
DR   OMA; LCTEWDE; -.
DR   OrthoDB; 647136at2; -.
DR   BioCyc; BHEL693979:G1GQY-2355-MONOMER; -.
DR   Proteomes; UP000008630; 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:UP000008630};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124,
KW   ECO:0000313|EMBL:ADV44299.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008630}.
FT   DOMAIN      320    422       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   437 AA;  48677 MW;  0467D7C425E21FA5 CRC64;
     MKIAIVGTGY VGLVTGTCFA EIGVNVVCVD TNSNKIKSLE KGIIPIYENG LEEMVIRNAK
     AGRLQFTTSL ESCLNDVDVV FSAVGTPPDE DGSADLSYVL EVARTIGRNM QKYVLVVTKS
     TVPVGTAQKV RSAIQDELDK RKIVIEFDVA SNPEFLKEGN AINDFMSPDR VVVGVESERA
     RKLMTKLYKP FLLNNFRVIF MDIPSAEMTK YAANSMLATR ISFMNDIANL CELVGADVNM
     VRSGIGSDTR IGRKFLYPGI GYGGSCFPKD VKALIKTAEQ TGYQMRVLQA VEEVNENQKN
     ILFEKLQKHF DNDLQGKTIA LWGLAFKPET DDMREAPALV LIDSLLKAGC KVRVYDPAAM
     NECRRRIGEL ICYATDMYDA ALDADALMLV TEWKEFRLPS WAVIKRTMKQ AVVLDGRNIY
     DKKEMEEQGF VYHCIGK
//
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