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Database: UniProt
Entry: A0A162PBK8_9BACT
LinkDB: A0A162PBK8_9BACT
Original site: A0A162PBK8_9BACT 
ID   A0A162PBK8_9BACT        Unreviewed;       439 AA.
AC   A0A162PBK8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   10-APR-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=A1D16_02110 {ECO:0000313|EMBL:KYP14293.1};
OS   Flavihumibacter sp. CACIAM 22H1.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Flavihumibacter.
OX   NCBI_TaxID=1812911 {ECO:0000313|EMBL:KYP14293.1, ECO:0000313|Proteomes:UP000075747};
RN   [1] {ECO:0000313|EMBL:KYP14293.1, ECO:0000313|Proteomes:UP000075747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CACIAM 22H1 {ECO:0000313|EMBL:KYP14293.1};
RA   Moraes P.G., Lima A.R.;
RT   "Draft Genome of Flavihumibacter sp. CACIAM 22H1.";
RL   Submitted (MAR-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:KYP14293.1}.
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DR   EMBL; LUKG01000046; KYP14293.1; -; Genomic_DNA.
DR   Proteomes; UP000075747; 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:UP000075747};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124}.
FT   DOMAIN      315    417       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   ACT_SITE    261    261       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     121    121       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     153    153       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     264    264       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     329    329       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
SQ   SEQUENCE   439 AA;  48512 MW;  52BD7A81A6492639 CRC64;
     MKITVVGTGY VGLVTGTCFA ETGNEVICVD IDQSKVDRLT NGEITIYEPG LEKLFLRNLK
     EGRLSFTTSL AEGIKEAAII FLALPTPPGA DGAADLKYVL GVSEEIGKLL TDYKVLVDKS
     TVPVGTADKV RAAVARNYAG EFDVVSNPEF LREGVAVDDF MKPDRVVIGV SSDRARKLMG
     ELYAPFVRSG NPVIYMDERS AELTKYAANS FLATKISFMN EVAQLCERLG ADVDMVRLGI
     GSDDRIGKRF LFPGIGYGGS CFPKDVQALV QSSAQAEYDF KILNAVMEVN EKQKTHLLPK
     IRRYYGNALK GRHFALWGLA FKPNTDDIRE APALYMIDAL LAEGATITAF DPEAIRNVKQ
     LLGDKIRYAD NQYDALQDAD ALLIATEWNE FRTPDFLKMV TRMKSKVIFD GRNLFDIRAI
     SELGFHYESI GRKTVSNSK
//
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