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Database: UniProt
Entry: A0A0K2E003_PISSA
LinkDB: A0A0K2E003_PISSA
Original site: A0A0K2E003_PISSA 
ID   A0A0K2E003_PISSA        Unreviewed;       449 AA.
AC   A0A0K2E003;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-FEB-2019, entry version 15.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=KW89_2437 {ECO:0000313|EMBL:ALA25899.1};
OS   Piscirickettsia salmonis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Piscirickettsia.
OX   NCBI_TaxID=1238 {ECO:0000313|EMBL:ALA25899.1, ECO:0000313|Proteomes:UP000029541};
RN   [1] {ECO:0000313|EMBL:ALA25899.1, ECO:0000313|Proteomes:UP000029541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1-15972 {ECO:0000313|Proteomes:UP000029541};
RA   Babu N.S., Beckwith C.J., Beseler K.G., Brison A., Carone J.V.,
RA   Caskin T.P., Diamond M., Durham M.E., Foxe J.M., Go M.,
RA   Henderson B.A., Jones I.B., McGettigan J.A., Micheletti S.J.,
RA   Nasrallah M.E., Ortiz D., Piller C.R., Privatt S.R., Schneider S.L.,
RA   Sharp S., Smith T.C., Stanton J.D., Ullery H.E., Wilson R.J.,
RA   Serrano M.G., Buck G., Lee V., Wang Y., Carvalho R., Voegtly L.,
RA   Shi R., Duckworth R., Johnson A., Loviza R., Walstead R., Shah Z.,
RA   Kiflezghi M., Wade K., Ball S.L., Bradley K.W., Asai D.J.,
RA   Bowman C.A., Russell D.A., Pope W.H., Jacobs-Sera D., Hendrix R.W.,
RA   Hatfull G.F.;
RL   Submitted (AUG-2015) 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}.
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DR   EMBL; CP012413; ALA25899.1; -; Genomic_DNA.
DR   RefSeq; WP_036779883.1; NZ_CP013773.1.
DR   EnsemblBacteria; ALA25899; ALA25899; KW89_2437.
DR   OrthoDB; 647136at2; -.
DR   BioCyc; GCF_001932595:G1FKG-516-MONOMER; -.
DR   BioCyc; GCF_001932735:G1FKM-636-MONOMER; -.
DR   BioCyc; GCF_001932755:G1FKO-1470-MONOMER; -.
DR   BioCyc; GCF_001932775:G1FKP-1466-MONOMER; -.
DR   Proteomes; UP000029541; 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:UP000029541};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124,
KW   ECO:0000313|EMBL:ALA25899.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029541}.
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   449 AA;  49363 MW;  C0C75A1496F83599 CRC64;
     MRVTVFGAGY VGLVTAACFA DLGNQVICVD VDEKKLAQLA EGKSPIYEPG LDELLLRGQE
     SGNLEFTADI QSAVEQGEFI FIAVGTPSEE SGSADLQYVL AVAKSIGEYM NGYKLVIDKS
     TVPLGTADKV RQVISNELGA RGVNYEFDVS SNPEFLKEGA AIEDFMYPDR VVIGIDNLRA
     EKRLKTLYTP LTKKNNCLVV MDVRSAELTK YAANAMLATK ISFMNEMSQL AERVGADIEM
     VRQGIGSDSR IGYHFIYPGC GYGGSCFPKD VRALVHTAAE HGFDTKILGA VQEVNEKQKE
     LLLEKVLREF QGDIQGKTFA LWGLAFKPKT DDIREAPSRV LMEGLWQHGA KVQAYDPAAM
     DNIQAVYGAR DDLYLATSAS SALTGADALI VVTEWTEFRS PDFNVIKKTL NQPLVIDGRN
     IYDAEHLESL GITYRCIGRG EWLMKDVCR
//
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