KDGK_HAEIN
ID KDGK_HAEIN Reviewed; 314 AA.
AC P44482;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=2-dehydro-3-deoxygluconokinase;
DE EC=2.7.1.45;
DE AltName: Full=2-keto-3-deoxygluconokinase;
DE AltName: Full=3-deoxy-2-oxo-D-gluconate kinase;
DE AltName: Full=KDG kinase;
GN Name=kdgK; OrderedLocusNames=HI_0049;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate
CC (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-gluconate + ATP = 2-dehydro-3-deoxy-6-
CC phospho-D-gluconate + ADP + H(+); Xref=Rhea:RHEA:14797,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57569,
CC ChEBI:CHEBI:57990, ChEBI:CHEBI:456216; EC=2.7.1.45;
CC -!- PATHWAY: Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate
CC degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-
CC 3-deoxy-D-gluconate: step 1/2.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; L42023; AAC21727.1; -; Genomic_DNA.
DR PIR; C64045; C64045.
DR RefSeq; NP_438222.1; NC_000907.1.
DR RefSeq; WP_005693872.1; NC_000907.1.
DR AlphaFoldDB; P44482; -.
DR SMR; P44482; -.
DR STRING; 71421.HI_0049; -.
DR EnsemblBacteria; AAC21727; AAC21727; HI_0049.
DR KEGG; hin:HI_0049; -.
DR PATRIC; fig|71421.8.peg.49; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_8_0_6; -.
DR OMA; DDEQLIW; -.
DR PhylomeDB; P44482; -.
DR BioCyc; HINF71421:G1GJ1-50-MON; -.
DR UniPathway; UPA00856; UER00828.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0019698; P:D-galacturonate catabolic process; IBA:GO_Central.
DR GO; GO:0042840; P:D-glucuronate catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="2-dehydro-3-deoxygluconokinase"
FT /id="PRO_0000080087"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 28..32
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 102..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 168..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 228..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 260..263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ SEQUENCE 314 AA; 35462 MW; 24CA631C8B0485F9 CRC64;
MKKIAFIGEC MIELNGKPFA EMWQSYGGDT LNSATYLSRV SSSKEIQVHY VSALGTDNLS
KQMLKYWQAD GIQTNWVLQD EQHQPGLYLI QLDAQGERTF LYWRNQSAAR YMVQHPDFAK
VIAELQQVDV IYLSGISLAI LPKNDRTFLI EQLSSLAKKG TEIVFDSNYR PKLWDSLEEA
QDCYLQLLPS VNIALVTFDD EQALWKDKTS RDTLERLHKI GIPKVIVKCG KNGAIFSDRY
LSQYGQVIPE PILNVVDTTS AGDSFNAGFL NGYLRNKSLE ICCQQGNRIA GIVIQHKGAI
IDKVAISHLQ SEFN
