KDUD_BACSU
ID KDUD_BACSU Reviewed; 254 AA.
AC P50842;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase;
DE EC=1.1.1.127;
DE AltName: Full=2-keto-3-deoxygluconate 5-dehydrogenase;
DE AltName: Full=2-keto-3-deoxygluconate oxidoreductase;
DE Short=KDG oxidoreductase;
GN Name=kduD; OrderedLocusNames=BSU22140;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
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).
RN [3]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=17322190; DOI=10.1099/mic.0.2006/002253-0;
RA Lin J.S., Shaw G.C.;
RT "Regulation of the kduID operon of Bacillus subtilis by the KdgR repressor
RT and the ccpA gene: identification of two KdgR-binding sites within the
RT kdgR-kduI intergenic region.";
RL Microbiology 153:701-710(2007).
CC -!- FUNCTION: Catalyzes the reduction of 2,5-diketo-3-deoxygluconate (DKII
CC or 4,6-dihydroxy-2,5-dioxohexanoate) into 2-keto-3-deoxygluconate (KDG
CC or 2-dehydro-3-deoxygluconate) with a concomitant oxidation of NADH.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate + NAD(+) = 3-deoxy-D-glycero-
CC 2,5-hexodiulosonate + H(+) + NADH; Xref=Rhea:RHEA:24232,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29071, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57990; EC=1.1.1.127;
CC -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 5/5.
CC -!- INDUCTION: Induced by galacturonate and negatively regulated by the
CC KdgR repressor. Is subject to catabolite repression by glucose
CC involving the ccpA gene. {ECO:0000269|PubMed:17322190}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; L47838; AAB38476.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14131.1; -; Genomic_DNA.
DR PIR; D69648; D69648.
DR RefSeq; NP_390096.1; NC_000964.3.
DR RefSeq; WP_003230720.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P50842; -.
DR SMR; P50842; -.
DR STRING; 224308.BSU22140; -.
DR jPOST; P50842; -.
DR PaxDb; P50842; -.
DR PRIDE; P50842; -.
DR EnsemblBacteria; CAB14131; CAB14131; BSU_22140.
DR GeneID; 939059; -.
DR KEGG; bsu:BSU22140; -.
DR PATRIC; fig|224308.179.peg.2418; -.
DR eggNOG; COG1028; Bacteria.
DR InParanoid; P50842; -.
DR OMA; QANLMTI; -.
DR PhylomeDB; P50842; -.
DR BioCyc; BSUB:BSU22140-MON; -.
DR UniPathway; UPA00545; UER00827.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0047001; F:2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008678; F:2-deoxy-D-gluconate 3-dehydrogenase activity; IEA:InterPro.
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:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011286; 2-deoxy-D-gluc_3_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01832; kduD; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..254
FT /note="2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase"
FT /id="PRO_0000054714"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 254 AA; 27186 MW; 245C57CF5CA46597 CRC64;
MGYLHDAFSL KGKTALVTGP GTGIGQGIAK ALAGAGADII GTSHTSSLSE TQQLVEQEGR
IFTSFTLDMS KPEAIKDSAA ELFENRQIDI LVNNAGIIHR EKAEDFPEEN WQHVLNVNLN
SLFILTQLAG RHMLKRGHGK IINIASLLSF QGGILVPAYT ASKHAVAGLT KSFANEWAAS
GIQVNAIAPG YISTANTKPI RDDEKRNEDI LKRIPAGRWG QADDIGGTAV FLASRASDYV
NGHILAVDGG WLSR
