GenomeNet

Database: UniProt
Entry: A0A0Q9AHH0_9ACTN
LinkDB: A0A0Q9AHH0_9ACTN
Original site: A0A0Q9AHH0_9ACTN 
ID   A0A0Q9AHH0_9ACTN        Unreviewed;       447 AA.
AC   A0A0Q9AHH0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   10-APR-2019, entry version 14.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   ORFNames=ASE41_21315 {ECO:0000313|EMBL:KRD17269.1};
OS   Streptomyces sp. Root264.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD17269.1, ECO:0000313|Proteomes:UP000051177};
RN   [1] {ECO:0000313|EMBL:KRD17269.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD17269.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD17269.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD17269.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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}.
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:KRD17269.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; LMIZ01000016; KRD17269.1; -; Genomic_DNA.
DR   RefSeq; WP_057578526.1; NZ_LMIZ01000016.1.
DR   EnsemblBacteria; KRD17269; KRD17269; ASE41_21315.
DR   Proteomes; UP000051177; 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:UP000051177};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051177}.
FT   DOMAIN      328    429       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    271    271       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR500134-1}.
FT   BINDING      32     32       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      37     37       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING      93     93       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     129    129       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     163    163       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     274    274       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     342    342       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   447 AA;  48328 MW;  395F25EE32056333 CRC64;
     MALNITVIGT GYLGATHAAA MAELGFEVLA LDVVREKIEM LERGETPMYE PGLEELLRRH
     VAGFEGSSGR LRFTQDWAEV GAFGDVHFVC VNTPQKHGEY ACDMSYVESA LASLAPHLTR
     PALVVGKSTV PVGSADRLAR MIAELAPAGE DAELAWNPEF LREGFAVQDT LHPDRIVVGV
     RSERAEALLR QVYETPVGEG SPFVVTDFPT AELVKTSANS FLATKISFIN AMAEVCEAAD
     GDVAKLAEAI GYDDRIGKKF LRAGIGFGGG CLPKDIRAFM ARAGELGADQ ALTFLREIDS
     INMRQRGRMV ELARQALGGG SFLGRRIAVL GATFKPDSDD VRDSPALNVA GQIHLQGGQV
     TVYDPKGMEN ARRLFPTLGY APSALDAVRG ADAVLHLTEW REFRELDPAA LGEVATTRLI
     LDGRNALDPE LWRKAGWTYR GMGRPTA
//
DBGET integrated database retrieval system