(data stored in ACNUC7421 zone)

SWISSPROT: Q3IEI5_PSEHT

ID   Q3IEI5_PSEHT            Unreviewed;       388 AA.
AC   Q3IEI5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   SubName: Full=UDP-glucose 6-dehydrogenase {ECO:0000313|EMBL:CAI85541.1};
DE            EC=1.1.1.22 {ECO:0000313|EMBL:CAI85541.1};
GN   Name=ugd {ECO:0000313|EMBL:CAI85541.1};
GN   OrderedLocusNames=PSHAa0444 {ECO:0000313|EMBL:CAI85541.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85541.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85541.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000124}.
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DR   EMBL; CR954246; CAI85541.1; -; Genomic_DNA.
DR   RefSeq; WP_011327154.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEI5; -.
DR   STRING; 326442.PSHAa0444; -.
DR   EnsemblBacteria; CAI85541; CAI85541; PSHAa0444.
DR   KEGG; pha:PSHAa0444; -.
DR   PATRIC; fig|326442.8.peg.421; -.
DR   eggNOG; ENOG4107RHE; Bacteria.
DR   eggNOG; COG1004; LUCA.
DR   HOGENOM; HOG000280378; -.
DR   KO; K00012; -.
DR   OMA; ANVCFIF; -.
DR   OrthoDB; POG091H04WU; -.
DR   Proteomes; UP000006843; Chromosome I.
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   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR013328; 6PGD_dom_2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
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; 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;
DR   PRODOM; Q3IEI5.
DR   SWISS-2DPAGE; Q3IEI5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   NAD {ECO:0000256|PIRSR:PIRSR500134-3};
KW   Oxidoreductase {ECO:0000313|EMBL:CAI85541.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN      300    387       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     306    306       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR500134-2}.
FT   BINDING     307    307       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
FT   BINDING     314    314       NAD. {ECO:0000256|PIRSR:PIRSR500134-3}.
FT   BINDING     388    388       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR500134-2}.
SQ   SEQUENCE   388 AA;  43416 MW;  E7DAEABE1FF01AC6 CRC64;
     MKVTVVGTGY VGLSNAMLLA QHNEVIALDI DEQKIALLNN KQSPIVDFHI SEYLQRDDIS
     FTATTNKSMA YCNADFIIIA TPTDYDTHTH NFNTSSVEAV INDALAYNPH AVIIVKSTVP
     VRFTQRMKAQ LGVDNIIFSP EFLREGKALY DNLHPSRIVV GEQSERAAVF ANLLKQGAIK
     QDIAVLFTES TEAEAIKLFS NTYLAMRVAY FNELDTYAEA HGLNSKQIIQ GVGLDPRIGN
     HYNNPSFGYG GYCLPKDTKQ LLANYKDIPN NMICAIVDAN TTRKNFIADS IIKRNPKVVG
     IYRLVMKTGS DNFRASAIQG IMKRIAASNV QMVVYEPELK EDVFYNSRVI RNLNEFKQIS
     DVVVSNRMVE ELSDITDKVY TRDLFGSD
//

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