(data stored in SCRATCH 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   08-MAY-2019, entry version 71.
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;
OC   Saccharomycetes; 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.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   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-
CC       phosphogluconate to ribulose 5-phosphate and CO(2), with
CC       concomitant reduction of NADP to NADPH.
CC       {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-
CC         phosphate + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58121, ChEBI:CHEBI:58349,
CC         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):
CC       step 3/3. {ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase
CC       family. {ECO:0000256|PIRNR:PIRNR000109,
CC       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; EGEPCVT; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000002036};
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       6PGD. {ECO:0000259|SMART:SM01350}.
FT   NP_BIND      12     17       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      35     37       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   NP_BIND      77     79       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   REGION      131    133       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   REGION      188    189       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   ACT_SITE    185    185       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   ACT_SITE    192    192       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000109-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000109-3}.
FT   BINDING     105    105       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     193    193       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     289    289       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000109-2}.
FT   BINDING     449    449       Substrate; shared with dimeric partner.
FT                                {ECO:0000256|PIRSR:PIRSR000109-2}.
FT   BINDING     455    455       Substrate; shared with dimeric partner.
FT                                {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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