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Database: UniProt
Entry: B2V606_SULSY
LinkDB: B2V606_SULSY
Original site: B2V606_SULSY 
ID   B2V606_SULSY            Unreviewed;       389 AA.
AC   B2V606;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=UDP-glucose 6-dehydrogenase {ECO:0000256|PIRNR:PIRNR000124};
DE            EC=1.1.1.22 {ECO:0000256|PIRNR:PIRNR000124};
GN   OrderedLocusNames=SYO3AOP1_1498 {ECO:0000313|EMBL:ACD67100.1};
OS   Sulfurihydrogenibium sp. (strain YO3AOP1).
OC   Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Sulfurihydrogenibium.
OX   NCBI_TaxID=436114 {ECO:0000313|EMBL:ACD67100.1, ECO:0000313|Proteomes:UP000001201};
RN   [1] {ECO:0000313|Proteomes:UP000001201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YO3AOP1 {ECO:0000313|Proteomes:UP000001201};
RX   PubMed=19136599; DOI=10.1128/JB.01645-08;
RA   Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA   Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA   Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT   "Complete and draft genome sequences of six members of the
RT   Aquificales.";
RL   J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD67100.1; -; Genomic_DNA.
DR   RefSeq; WP_012460157.1; NC_010730.1.
DR   STRING; 436114.SYO3AOP1_1498; -.
DR   EnsemblBacteria; ACD67100; ACD67100; SYO3AOP1_1498.
DR   KEGG; sul:SYO3AOP1_1498; -.
DR   eggNOG; ENOG4105C6Y; Bacteria.
DR   eggNOG; COG1004; LUCA.
DR   HOGENOM; HOG000280378; -.
DR   KO; K00012; -.
DR   OMA; YRAMGRP; -.
DR   OrthoDB; 647136at2; -.
DR   BioCyc; SSP436114:G1GC2-1550-MONOMER; -.
DR   Proteomes; UP000001201; 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; 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:UP000001201};
KW   NAD {ECO:0000256|PIRNR:PIRNR000124, ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000124,
KW   ECO:0000313|EMBL:ACD67100.1}.
FT   DOMAIN      302    388       UDPG_MGDP_dh_C. {ECO:0000259|SMART:
FT                                SM00984}.
FT   REGION      142    145       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   REGION      242    246       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   ACT_SITE    253    253       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      83     83       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     118    118       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     145    145       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     197    197       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     250    250       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     256    256       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     308    308       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     309    309       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     316    316       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     389    389       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
SQ   SEQUENCE   389 AA;  44107 MW;  87B82176F10058E1 CRC64;
     MKIAVAGAGY VGLSNAILLA QNHQVVIKDI DPQKVKLINE KKSPIIDKDI QEYLATKNLN
     IKATLDPQEA YKDAKYVIIA TPTDYDPITN YFNTKSVESV IKEVLTVNPD AVMVIKSTIP
     IGYTESIKKK FNTENIIFSP EFLREGKALY DNLYPSRVVV GEKSERAKEF ANLLLEGAIK
     KDVPVLFTGS TEAESIKLFA NTYLAMRVAF FNELDTFAES HGLNSKEIIE GVCLDPRIGM
     HYNNPSFGFG GYCLPKDTKQ LMANYLEKGI PHFLIKATVE SNIARKYYIA EKIISLNPKI
     VGVYRLTMKS DSDNFREAAI IDIIEYLRAK DVQVIIFEPL LKESKFMDFD VVSLERLKKE
     SDIILANRYS SDLDDVREKV YTRDVFYRD
//
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