(data stored in ACNUC8465 zone)

SWISSPROT: C5DD65_LACTC

ID   C5DD65_LACTC            Unreviewed;       492 AA.
AC   C5DD65;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
DE            EC=1.1.1.44 {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
GN   OrderedLocusNames=KLTH0B08668g {ECO:0000313|EMBL:CAR21726.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21726.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21726.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC       to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC       to NADPH. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC         + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000109,
CC         ECO:0000256|RuleBase:RU000485};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC       3/3. {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485}.
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DR   EMBL; CU928166; CAR21726.1; -; Genomic_DNA.
DR   RefSeq; XP_002552164.1; XM_002552118.1.
DR   STRING; 381046.XP_002552164.1; -.
DR   EnsemblFungi; CAR21726; CAR21726; KLTH0B08668g.
DR   GeneID; 8291005; -.
DR   KEGG; lth:KLTH0B08668g; -.
DR   HOGENOM; HOG000255147; -.
DR   InParanoid; C5DD65; -.
DR   KO; K00033; -.
DR   OMA; PRKILVM; -.
DR   OrthoDB; 847823at2759; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006114; 6PGDH_C.
DR   InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR006184; 6PGdom_BS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR006183; Pgluconate_DH.
DR   PANTHER; PTHR11811; PTHR11811; 1.
DR   Pfam; PF00393; 6PGD; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000109; 6PGD; 1.
DR   PRINTS; PR00076; 6PGDHDRGNASE.
DR   SMART; SM01350; 6PGD; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00873; gnd; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD65.
DR   SWISS-2DPAGE; C5DD65.
KW   Gluconate utilization {ECO:0000256|RuleBase:RU000485};
KW   NADP {ECO:0000256|PIRNR:PIRNR000109, ECO:0000256|RuleBase:RU000485};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Pentose shunt {ECO:0000256|PIRNR:PIRNR000109,
KW   ECO:0000256|RuleBase:RU000485};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN          181..479
FT                   /note="6PGD"
FT                   /evidence="ECO:0000259|SMART:SM01350"
FT   NP_BIND         12..17
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   NP_BIND         35..37
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   NP_BIND         77..79
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   REGION          131..133
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   REGION          188..189
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   ACT_SITE        192
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-1"
FT   BINDING         105
FT                   /note="NADP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         105
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         193
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         262
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         289
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         449
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         455
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ   SEQUENCE   492 AA;  53976 MW;  D5599273C6CAACF8 CRC64;
     MAQPKGDMGL IGLAVMGQNL ILNAADHGYT VVAFNRTVSK VDHFMENEAK GKSIIGAHSI
     QELVDNLKRP RRIVLLVKAG AAVDAFIEQL LPYLEKGDII IDGGNSHYPD TNRRYEELKG
     KGIYFVGSGV SGGEEGARYG PSLMPGGAEE AWPHIKEIFQ AISAKSDGEP CCDWVGPAGA
     GHYVKMVHNG IEYGDMQLIT EAYDIMKRVG GFSDKEIGDV FAKWNTGVLD SFLVEITRDI
     LRYDDKDGTP LVEKIMDSAG QKGTGKWTAI NALDLGMPVT LIGEAVFARC LSSLKSERIR
     AASILPGPEV SKDAIKDKQQ FVDDLEQALY ASKIISYAQG FMLIREAGKT YNWKLNNPAI
     ALMWRGGCII RSVFLAEITK AYRENPELEN LLFNKFFTDA ITKAQSGWRK TIALASTQGI
     PTPAFSTALS FYDGYRSERL PANLLQAQRD YFGAHTFRVL PECASEDLPE GQDIHVNWTG
     RGGNISASTY QA
//

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