2KGR_GLUOX
ID 2KGR_GLUOX Reviewed; 310 AA.
AC Q5FTU6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=2-ketogluconate reductase {ECO:0000303|PubMed:20676631};
DE Short=2KGR {ECO:0000303|PubMed:17928715, ECO:0000303|PubMed:20676631};
DE EC=1.1.1.215 {ECO:0000269|PubMed:20676631};
DE AltName: Full=Gluconate 2-dehydrogenase {ECO:0000305};
GN OrderedLocusNames=GOX0417 {ECO:0000312|EMBL:AAW60200.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
RN [2]
RP PROTEIN SEQUENCE OF 2-11.
RC STRAIN=ATCC 621 / DSM 50049 / NBRC 3172 / NCIMB 7069 / NRRL B-72;
RX PubMed=17928715; DOI=10.1271/bbb.70259;
RA Saichana I., Ano Y., Adachi O., Matsushita K., Toyama H.;
RT "Preparation of enzymes required for enzymatic quantification of 5-keto-D-
RT gluconate and 2-keto-D-gluconate.";
RL Biosci. Biotechnol. Biochem. 71:2478-2486(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=621H;
RX PubMed=20676631; DOI=10.1007/s00253-010-2779-9;
RA Rauch B., Pahlke J., Schweiger P., Deppenmeier U.;
RT "Characterization of enzymes involved in the central metabolism of
RT Gluconobacter oxydans.";
RL Appl. Microbiol. Biotechnol. 88:711-718(2010).
CC -!- FUNCTION: Catalyzes the reduction of 2-keto-D-gluconate to gluconate.
CC Can also catalyze the reduction of 2-keto-L-gulonate. Can use both NADH
CC and NADPH efficiently, with a slight preference for NADPH.
CC {ECO:0000269|PubMed:20676631}.
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; Evidence={ECO:0000269|PubMed:20676631};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.16 mM for 2-ketogluconate {ECO:0000269|PubMed:20676631};
CC KM=51.5 uM for NADH {ECO:0000269|PubMed:20676631};
CC KM=10 uM for NADPH {ECO:0000269|PubMed:20676631};
CC Vmax=86.7 umol/min/mg enzyme {ECO:0000269|PubMed:20676631};
CC Note=kcat is 48.2 sec(-1). {ECO:0000269|PubMed:20676631};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:20676631}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CP000009; AAW60200.1; -; Genomic_DNA.
DR RefSeq; WP_011252001.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FTU6; -.
DR SMR; Q5FTU6; -.
DR STRING; 290633.GOX0417; -.
DR EnsemblBacteria; AAW60200; AAW60200; GOX0417.
DR KEGG; gox:GOX0417; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR OMA; NVPDYCM; -.
DR BRENDA; 1.1.1.215; 38.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0008873; F:gluconate 2-dehydrogenase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW Direct protein sequencing; Gluconate utilization; NAD; NADP;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:17928715"
FT CHAIN 2..310
FT /note="2-ketogluconate reductase"
FT /id="PRO_0000434438"
FT ACT_SITE 229
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT ACT_SITE 258
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT ACT_SITE 276
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 151..152
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT BINDING 227..229
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9I3W9"
FT CONFLICT 9
FT /note="T -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 33146 MW; 1B3F1F4304B5FC3E CRC64;
MSSKPDILTI DPLVPVMKER LEKSFTLHPY TSLENLKNIA PAIRGITTGG GSGVPSEIMD
ALPNLEVISV NGVGTDRINL DEARRRNIGV AITQNTLTDD VADMAVALMM AVMRSIVTND
AFVRAGKWPS ATAPLGRSLT RKKVGIAGFG HIGQAIAKRV SAFGMEVAYF NSHARPESTC
HFEPDLKALA TWCDVLILAV SGGPRSANMI DRDTLDALGK DGFLVNIARG TVVDEAALLS
ALQEKRIAGA GLDVFQNEPN INPAFLSLPN TVLQAHQASA TVETRTTMAN LVVDNLIAYF
TDKTLLTPVI
