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Database: UniProt
Entry: J6EMP5_SACK1
LinkDB: J6EMP5_SACK1
Original site: J6EMP5_SACK1 
ID   J6EMP5_SACK1            Unreviewed;       492 AA.
AC   J6EMP5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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   Name=YGR256W {ECO:0000313|EMBL:EJT44272.1};
GN   Synonyms=SKDI07G5060 {ECO:0000313|EMBL:CAI4063002.1};
GN   ORFNames=SKDI_07G5060 {ECO:0000313|EMBL:CAI4063002.1}, SKUD_199902
GN   {ECO:0000313|EMBL:EJT44272.1};
OS   Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS   NBRC 1802 / NCYC 2889) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT44272.1, ECO:0000313|Proteomes:UP000002753};
RN   [1] {ECO:0000313|EMBL:EJT44272.1, ECO:0000313|Proteomes:UP000002753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC   {ECO:0000313|EMBL:EJT44272.1};
RX   PubMed=12775844; DOI=10.1126/science.1084337;
RA   Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA   Waterston R., Cohen B.A., Johnston M.;
RT   "Finding functional features in Saccharomyces genomes by phylogenetic
RT   footprinting.";
RL   Science 301:71-76(2003).
RN   [2] {ECO:0000313|EMBL:EJT44272.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT44272.1};
RA   Cliften P.F., Johnston M.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000002753}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC   {ECO:0000313|Proteomes:UP000002753};
RX   PubMed=22384314; DOI=10.1534/g3.111.000273;
RA   Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA   Rine J., Johnston M., Hittinger C.T.;
RT   "The awesome power of yeast evolutionary genetics: New genome sequences and
RT   strain resources for the Saccharomyces sensu stricto genus.";
RL   G3 (Bethesda) 1:11-25(2011).
RN   [4] {ECO:0000313|EMBL:EJT44272.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT44272.1};
RA   Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA   Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:CAI4063002.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4063002.1};
RA   Byrne P K.;
RL   Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00002526,
CC       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|ARBA:ARBA00000530,
CC         ECO:0000256|PIRNR:PIRNR000109, 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|ARBA:ARBA00004874, ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC       ECO:0000256|PIRNR:PIRNR000109}.
CC   -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00008419, ECO:0000256|PIRNR:PIRNR000109,
CC       ECO:0000256|RuleBase:RU000485}.
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DR   EMBL; OX365902; CAI4063002.1; -; Genomic_DNA.
DR   EMBL; AACI03000404; EJT44272.1; -; Genomic_DNA.
DR   AlphaFoldDB; J6EMP5; -.
DR   STRING; 226230.J6EMP5; -.
DR   HOGENOM; CLU_024540_4_2_1; -.
DR   UniPathway; UPA00115; UER00410.
DR   Proteomes; UP000002753; Unassembled WGS sequence.
DR   Proteomes; UP001162087; Chromosome 7.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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   NCBIfam; TIGR00873; gnd; 1.
DR   PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11811:SF25; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00461; 6PGD; 1.
PE   3: Inferred from homology;
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064,
KW   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|ARBA:ARBA00023126,
KW   ECO:0000256|PIRNR:PIRNR000109};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002753}.
FT   DOMAIN          181..479
FT                   /note="6-phosphogluconate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01350"
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         12..17
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         35..37
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         77..79
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-3"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         131..133
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         188..189
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         289
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         449
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
FT   BINDING         455
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000109-2"
SQ   SEQUENCE   492 AA;  53949 MW;  DFDEA17BE8E37B03 CRC64;
     MSKAVGDLGL IGLAVMGQNL ILNAADHGFT VVAYNRTQSK VDRFLADEAK GKSIIGATSI
     RDLVAKLKKP RKIMILIKAG APVDNLIKEL VPHLDKGDII IDGGNSHFPD SNRHYEELTR
     QGILFVGSGV SGGEDGARFG PSLMPGGSEE AWPHIKDIFQ SIAAKSDGEP CCEWVGPAGS
     GHYVKMVHNG IEYGDMQLIC EAYDIMKRIG RFTDKEISEV FEKWNNGVLD SFLIEITRDI
     LKFDDVDGKP LVEKIMDTAG QKGTGKWTAI NALDLGMPVT LIGEAVFARC LSAIKDERKR
     ASKLLAGPTV PKDAIDDRQQ FVCDLEQALY ASKIISYAQG FMLIREAARS YGWKLNNPAI
     ALMWRGGCII RSVFLAEITK AYRNDPDLEN LLFNKFFASA ATKAQSGWRR SIALAATYGI
     PTPAFSTALA FYDGYRSERL PANLLQAQRD YFGAHTFRIL PECSSAHLPV DKDIHINWTG
     HGGNISSSTY QA
//
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