TKRA_BACSU
ID TKRA_BACSU Reviewed; 325 AA.
AC O32264; O06982;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable 2-ketogluconate reductase;
DE Short=2KR;
DE EC=1.1.1.215;
GN Name=yvcT; OrderedLocusNames=BSU34680;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB08066.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z94043; CAB08066.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15473.1; -; Genomic_DNA.
DR PIR; H70032; H70032.
DR RefSeq; NP_391348.1; NC_000964.3.
DR RefSeq; WP_010886621.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32264; -.
DR SMR; O32264; -.
DR STRING; 224308.BSU34680; -.
DR jPOST; O32264; -.
DR PaxDb; O32264; -.
DR PRIDE; O32264; -.
DR EnsemblBacteria; CAB15473; CAB15473; BSU_34680.
DR GeneID; 936519; -.
DR KEGG; bsu:BSU34680; -.
DR PATRIC; fig|224308.43.peg.3632; -.
DR eggNOG; COG1052; Bacteria.
DR InParanoid; O32264; -.
DR OMA; VHHQTLG; -.
DR PhylomeDB; O32264; -.
DR BioCyc; BSUB:BSU34680-MON; -.
DR Proteomes; UP000001570; Chromosome.
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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW Gluconate utilization; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..325
FT /note="Probable 2-ketogluconate reductase"
FT /id="PRO_0000076032"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT ACT_SITE 269
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 238..240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 288..291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 36619 MW; 53CAD7C378F2C0AF CRC64;
MLKPFVFITK PIPEEIEAFI GEHCRYEVWQ EDTLPSDVLF EKLKEAEGLL TSGTSGPSIN
RELLEHAPKL KVVSNQSVGY DNFDIEAMKE RGVVGTHTPY TLDDTVADLA FSLILSSARR
VAELDRFVRA GKWGTVEEEA LFGIDVHHQT LGIIGMGRIG EQAARRAKFG FDMEVLYHNR
HRKQETEDSI GVKYAELDTL LEQSDFILLI TPLTDETYHM IGEREFKLMK NSAIFVNISR
GKTVDEKALI RALQEGWIRG AGLDVYEKEP VTQDNPLLQL DNVTLLPHIG SATAKVRFNM
CKQAAENMLA AIQGQTPKNL TREFQ
