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Database: UniProt
Entry: A0A261G8K2_9BIFI
LinkDB: A0A261G8K2_9BIFI
Original site: A0A261G8K2_9BIFI 
ID   A0A261G8K2_9BIFI        Unreviewed;       414 AA.
AC   A0A261G8K2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   10-APR-2019, entry version 6.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=BAQU_0401 {ECO:0000313|EMBL:OZG67757.1};
OS   Bifidobacterium aquikefiri.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1653207 {ECO:0000313|EMBL:OZG67757.1, ECO:0000313|Proteomes:UP000216451};
RN   [1] {ECO:0000313|EMBL:OZG67757.1, ECO:0000313|Proteomes:UP000216451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 28769 {ECO:0000313|EMBL:OZG67757.1,
RC   ECO:0000313|Proteomes:UP000216451};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the
RT   Bifidobacteriaceae family.";
RL   BMC Genomics 18:568-568(2017).
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:OZG67757.1}.
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DR   EMBL; MWXA01000003; OZG67757.1; -; Genomic_DNA.
DR   Proteomes; UP000216451; 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; 2.
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:UP000216451};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216451};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    414       UDP-glucose 6-dehydrogenase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012808390.
FT   DOMAIN      326    413       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   REGION      147    150       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   REGION      264    268       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   ACT_SITE    275    275       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      29     29       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      34     34       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      88     88       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     123    123       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     150    150       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     219    219       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     272    272       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     278    278       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     332    332       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     333    333       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     340    340       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     414    414       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
SQ   SEQUENCE   414 AA;  45832 MW;  60DAFBE05E4987BA CRC64;
     MKIAVAGTGY VGLSVALLLS QHNEVHALDI IPEKVEMLND GKSPIVDKEI TEFLDGNSTG
     SRPLNFQATL DPRQAYTGAD YAVVATPTNY DSQKNYFDTS SVEAAIAAIR EVNPTAWIVI
     KSTIPVGYTV DLRGKLQDDR LLFSPEFLRE GHALYDNLHP SRVVVGAPQD DAEARRAAEG
     FADLLIHGAA EGEVDRINAD GTSGIPRLVV GPTEAEAIKL FANTYLALRV AFFNELDTYA
     ETRGLQTQEI IDGVCLDPRI RADYNNPSFG YGGYCLPKDT KQLLANYDQV PQNLISGIVD
     ANRTRKDFIA TEIEQKIKGV EDPVVGIYRL TMKSGSDNFR QSAIQGVMKR IKARGITVVV
     YEPTLNDPDF FGSKVTHDLE DFKKQSDVIV ANRWNEDLVD VSHKVYTRDL FRRD
//
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