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Database: UniProt
Entry: A0A222XET6_9CELL
LinkDB: A0A222XET6_9CELL
Original site: A0A222XET6_9CELL 
ID   A0A222XET6_9CELL        Unreviewed;       441 AA.
AC   A0A222XET6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-DEC-2018, 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=CBP52_16550 {ECO:0000313|EMBL:ASR56441.1};
OS   Cellulomonas sp. PSBB021.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2003551 {ECO:0000313|EMBL:ASR56441.1, ECO:0000313|Proteomes:UP000214627};
RN   [1] {ECO:0000313|EMBL:ASR56441.1, ECO:0000313|Proteomes:UP000214627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSBB021 {ECO:0000313|EMBL:ASR56441.1,
RC   ECO:0000313|Proteomes:UP000214627};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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}.
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DR   EMBL; CP021430; ASR56441.1; -; Genomic_DNA.
DR   KEGG; cez:CBP52_16550; -.
DR   KO; K00012; -.
DR   Proteomes; UP000214627; Chromosome.
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:UP000214627};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214627}.
FT   DOMAIN      324    425       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    268    268       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     150    150       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     271    271       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     338    338       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   441 AA;  46775 MW;  8AD97EAEB420AF22 CRC64;
     MRISVIGCGY LGAVHAAAMA SLGHEVVGID VDERKIDALR AGRAPFFEPG LPELLLEAGA
     AGGLTFSTDI AAVAGARVHF VCVGTPQMKG EFRADMRYVD ASVTSLLPYL QPGDVVVGKS
     TVPVGTAERL AEQIAPTGAT LIWNPEFLRE GFAVEDTLHP DRFVYGLPTD EAGVVTAAGE
     AAKALLDEVY ATPLSDGTPL VVTDYPTAQL VKVAANSFLA TKISFINAMA ELCEATGGDV
     TQLADAIGYD VRIGRKFLNA GLGFGGGCLP KDIRAFMARA GELGVDQALT FLREVDSING
     RRRERMVELA REVCEGTLVG KRVAVLGATF KPNSDDIRDS PALAVADMLD KAGAHVVVTD
     PQGIENARAA RPDLHYADDV LDAVRDADVV LLGTEWAQYR ELDPDALAGV VAGRHILDGR
     NVLDPARWRA AGWTYRALGR P
//
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