TKRA_DICDI
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 03-AUG-2022, entry version 112.
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; Evosea; Eumycetozoa; Dictyostelia; 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., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., 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., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., 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 (IA).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-gluconate + NADP(+) = 2-dehydro-D-gluconate + H(+) + NADPH;
CC Xref=Rhea:RHEA:16653, ChEBI:CHEBI:15378, ChEBI:CHEBI:16808,
CC ChEBI:CHEBI:18391, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC 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}.
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DR EMBL; AAFI02000187; EAL61408.1; -; Genomic_DNA.
DR RefSeq; XP_629831.1; XM_629829.1.
DR AlphaFoldDB; 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 HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; Q54DP1; -.
DR OMA; PHIAWAY; -.
DR PhylomeDB; Q54DP1; -.
DR PRO; PR:Q54DP1; -.
DR Proteomes; UP000002195; Chromosome 6.
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: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 Cytoplasm; Gluconate utilization; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Probable 2-ketogluconate reductase"
FT /id="PRO_0000328017"
FT ACT_SITE 246
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 164..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 244..246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 294..297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="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
