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Database: UniProt
Entry: A0A1Y3MDP1_9MICC
LinkDB: A0A1Y3MDP1_9MICC
Original site: A0A1Y3MDP1_9MICC 
ID   A0A1Y3MDP1_9MICC        Unreviewed;       380 AA.
AC   A0A1Y3MDP1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   18-SEP-2019, entry version 11.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=B8W74_00065 {ECO:0000313|EMBL:OUM45692.1}, CI784_00080
GN   {ECO:0000313|EMBL:PPB47812.1};
OS   Arthrobacter agilis.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=37921 {ECO:0000313|EMBL:OUM45692.1, ECO:0000313|Proteomes:UP000195940};
RN   [1] {ECO:0000313|EMBL:PPB47812.1, ECO:0000313|Proteomes:UP000238766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.15723 {ECO:0000313|EMBL:PPB47812.1,
RC   ECO:0000313|Proteomes:UP000238766};
RX   PubMed=7547308; DOI=.1099/00207713-45-4-837;
RA   Koch C., Schumann P., Stackebrandt E.;
RT   "Reclassification of Micrococcus agilis (Ali-Cohen 1889) to the genus
RT   Arthrobacter as Arthrobacter agilis comb. nov. and emendation of the
RT   genus Arthrobacter.";
RL   Int. J. Syst. Bacteriol. 45:837-839(1995).
RN   [2] {ECO:0000313|EMBL:OUM45692.1, ECO:0000313|Proteomes:UP000195940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4042 {ECO:0000313|EMBL:OUM45692.1,
RC   ECO:0000313|Proteomes:UP000195940};
RA   Crovadore J., Blanc P., Chablais R., Cochard B., Grizard D.,
RA   Lefort F.;
RT   "Two whole genome sequences of Arthrobacter agilis isolates 4041 and
RT   4042 strain commercialized as biostimulants.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PPB47812.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CGMCC 1.15723 {ECO:0000313|EMBL:PPB47812.1};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) 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:OUM45692.1}.
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DR   EMBL; NFSD01000013; OUM45692.1; -; Genomic_DNA.
DR   EMBL; PRKX01000007; PPB47812.1; -; Genomic_DNA.
DR   Proteomes; UP000195940; Unassembled WGS sequence.
DR   Proteomes; UP000238766; 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:UP000195940,
KW   ECO:0000313|Proteomes:UP000238766};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195940}.
FT   DOMAIN      320    380       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    264    264       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      85     85       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     121    121       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     152    152       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     267    267       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     334    334       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   380 AA;  40775 MW;  8C7D42406FB85544 CRC64;
     MRISVIGCGY LGAVHAVCLA KLGHDVIGID IDLRKVGDLQ AARAPFFEPG LSELLDEVLM
     TGRLKFSPSM ADAKGSDVHF LCVGTPQRKG DYAADMRHVD SAFVSLLDFL EPGNLIVGKS
     TVPVGTAVRL ADQLSRRYPD GLLAWNPEFL REGLAIQDTL SPDRFVYGIP EGEDGTRAAQ
     LLDAVYATPL AAGVPRLCTN YATAELVKAA ANSFLATKIS YINAMAEVCE VTGADVTLLA
     DALGFDERIG RKFLNAGVGF GGGCLPKDIR AFMARVGELG ADQALTFLRE VDDINVRRRF
     RTVELTRTLV GNSLLGKRIT VLGAAFKPDS DDVRDSPALS IAAQLQLQGA EVTVTDPEAI
     DGARRRFPEL VYEEDLTGSS
//
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