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Database: UniProt
Entry: A0A1M3LJG9_9PROT
LinkDB: A0A1M3LJG9_9PROT
Original site: A0A1M3LJG9_9PROT 
ID   A0A1M3LJG9_9PROT        Unreviewed;       434 AA.
AC   A0A1M3LJG9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=BGO92_19550 {ECO:0000313|EMBL:OJX68611.1};
OS   Magnetospirillum sp. 64-120.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX68611.1, ECO:0000313|Proteomes:UP000184435};
RN   [1] {ECO:0000313|EMBL:OJX68611.1, ECO:0000313|Proteomes:UP000184435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=64-120 {ECO:0000313|EMBL:OJX68611.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA   Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA   Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process
RT   performance in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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}.
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:OJX68611.1}.
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DR   EMBL; MKVK01000046; OJX68611.1; -; Genomic_DNA.
DR   Proteomes; UP000184435; 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:UP000184435};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      317    418       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    263    263       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     122    122       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     155    155       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     266    266       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     331    331       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   434 AA;  46851 MW;  4E9D5522A300C6FF CRC64;
     MRIAMIGTGY VGLVSGTCFS EFGIDVVCVD KDAGKIEKLH QNIMPIYEPG LDELVADNVK
     AGRLSFTTDL KAAVKDADAV FIAVGTPSRR GDGHADLSYV YAAAEEIADA MTGYTVVVTK
     STVPVGTGDE VEAIIRKRRP DAQFDVVSNP EFLREGSAIN DFMRPDRVVI GTESDKARAV
     MKQLYRVLYL IETPIVFTSR RTSELIKYAG NTFLATKITF INEIADLCEK VGANVHDVAK
     GIGLDGRIGK KFLHPGPGYG GSCFPKDTLA LVKTARDYDA PLRIVETVVD VNDKRKKAMA
     ERVVAACGGS VAGKTVAVLG LTFKPNTDDM RDSPSLDIVP ALVAAGATVK AFDPEGMEEA
     KKLLSGITYC DDSYSTLQGA DVLVIVTEWN EFRALNLTKV KAALKAPVVV DLRNVYDPVE
     MREAGFTYSS IGRN
//
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