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Database: UniProt
Entry: Q54DP1
LinkDB: Q54DP1
Original site: Q54DP1 
ID   TKRA_DICDI              Reviewed;         334 AA.
AC   Q54DP1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   05-DEC-2018, entry version 99.
DE   RecName: Full=Probable 2-ketogluconate reductase;
DE            Short=2KR;
DE            EC=1.1.1.215;
DE   AltName: Full=2-ketoaldonate reductase;
GN   Name=tkrA; ORFNames=DDB_G0292104;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 2,5-diketo-D-
CC       gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-keto-D-gluconate
CC       (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate
CC       (IA). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:16653, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16808, ChEBI:CHEBI:18391, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.215;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; AAFI02000187; EAL61408.1; -; Genomic_DNA.
DR   RefSeq; XP_629831.1; XM_629829.1.
DR   ProteinModelPortal; Q54DP1; -.
DR   SMR; Q54DP1; -.
DR   STRING; 44689.DDB0231445; -.
DR   PaxDb; Q54DP1; -.
DR   EnsemblProtists; EAL61408; EAL61408; DDB_G0292104.
DR   GeneID; 8628512; -.
DR   KEGG; ddi:DDB_G0292104; -.
DR   dictyBase; DDB_G0292104; tkrA.
DR   eggNOG; KOG0069; Eukaryota.
DR   eggNOG; COG1052; LUCA.
DR   InParanoid; Q54DP1; -.
DR   KO; K00090; -.
DR   OMA; KWIAHNG; -.
DR   PhylomeDB; Q54DP1; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:Q54DP1; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0019521; P:D-gluconate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Gluconate utilization; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    334       Probable 2-ketogluconate reductase.
FT                                /FTId=PRO_0000328017.
FT   NP_BIND     164    165       NAD. {ECO:0000250}.
FT   NP_BIND     244    246       NAD. {ECO:0000250}.
FT   NP_BIND     294    297       NAD. {ECO:0000250}.
FT   ACT_SITE    246    246       {ECO:0000250}.
FT   ACT_SITE    275    275       {ECO:0000250}.
FT   ACT_SITE    294    294       Proton donor. {ECO:0000250}.
FT   BINDING     270    270       NAD. {ECO:0000250}.
SQ   SEQUENCE   334 AA;  37433 MW;  18F9A3028198998A CRC64;
     MTSIKNNNEN KHIVVYRKIH QSLIEKLENQ GYKVTQFEPI NSNNIQEFYE AIKTANGLIG
     SVFKIDENVL SKAPFLECVS AISVGYDNYD LVVLNDRKIP LMHTPNVLND SMADIMMGLM
     ITVARKLAYC DKRMRNGEWN GPLDKSWFGL EVHHKKVGII GMGRIGEVLA KRCRMGFDME
     VAYYSRSRHL KVEELYDAKH QDLDTILSTS DFICVVLPGS QETKHFFSFG QFSKMKNSAI
     FINAGRGMTV DEVALIDALE TGKIAGAGLD VFEKEPLNKD SKLLTLDNIV LLPHIGTSTI
     ETQHIMSECA VNNLISALNG NLEKNCVNAS IIKK
//
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