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Database: UniProt
Entry: A0A1F6NXJ4_9BACT
LinkDB: A0A1F6NXJ4_9BACT
Original site: A0A1F6NXJ4_9BACT 
ID   A0A1F6NXJ4_9BACT        Unreviewed;       461 AA.
AC   A0A1F6NXJ4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   16-JAN-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=A3J93_01000 {ECO:0000313|EMBL:OGH88657.1};
OS   Candidatus Magasanikbacteria bacterium RIFOXYC2_FULL_42_28.
OC   Bacteria; Candidatus Magasanikbacteria.
OX   NCBI_TaxID=1798704 {ECO:0000313|EMBL:OGH88657.1};
RN   [1] {ECO:0000313|EMBL:OGH88657.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U.,
RA   Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected
RT   biogeochemical processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGH88657.1}.
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DR   EMBL; MFQZ01000001; OGH88657.1; -; Genomic_DNA.
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   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      333    438       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    279    279       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      92     92       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     136    136       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     168    168       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     282    282       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     347    347       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   461 AA;  51328 MW;  B81312777D77B58B CRC64;
     MKILYIGSGF VGACSAAVSA NSGHETLAYD IDENKIAMLG ANDRDTIESC LFEEGLGDLI
     VRNREHLTFT SDYDKVEEFI EDVDAIFMCL PTPEIGETGE SDLKYYNSAT IKLAQILASR
     NTNKQSKYVV IVNKSTVPIN MVDQTAEIMK KQGVKNFGVV SNPEFLVEGK AVSGSLKPDR
     VVVGASSQKD FGIMRQIYRR FYDSTAIKYI EVNPKEAAAS KLLANFYLFN KLAVCFDVIG
     RACETFSDIK FENIRSILTS DKRIGDWGFY DSLYAGGSCF IKDARSLSHQ LQSAGQNATI
     VNETYLANKR QLNIFVGRAQ REANFDWSGK TVALFGTAFK QDTNDIRNSP SIDIVNYLME
     QSVKKINIFD PAALRWFKTI FPPSKQLIYV ANEIEALAGA DVVIIVTDWP QFRGLADVLL
     SGFKGRPLIM DGRRLWQHRY PDLQKAGFDI IAVGGVFLKG V
//
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