ID   KDGK_PSEA6              Reviewed;         318 AA.
AC   Q15UF1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=2-dehydro-3-deoxygluconokinase {ECO:0000305};
DE            EC=2.7.1.45 {ECO:0000269|Ref.2};
DE   AltName: Full=2-keto-3-deoxy-D-gluconate kinase {ECO:0000303|Ref.2};
DE   AltName: Full=2-keto-3-deoxygluconokinase {ECO:0000305};
DE   AltName: Full=3-deoxy-2-oxo-D-gluconate kinase {ECO:0000305};
DE   AltName: Full=KDG kinase {ECO:0000303|Ref.2};
GN   OrderedLocusNames=Patl_1969 {ECO:0000312|EMBL:ABG40487.1};
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA   Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=T6c / ATCC BAA-1087;
RX   DOI=10.1007/s12257-014-0622-3;
RA   Lee S.B., Cho S.J., Kim J.A., Lee S.Y., Kim S.M., Lim H.S.;
RT   "Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading
RT   microorganisms.";
RL   Biotechnol. Bioprocess Eng. 19:866-878(2014).
CC   -!- FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which
CC       is the major monomeric sugar of red macroalgae. Catalyzes the fifth
CC       step of the pathway, the phosphorylation of 2-keto-3-deoxygluconate
CC       (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDPG). {ECO:0000269|Ref.2}.
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         Evidence={ECO:0000269|Ref.2};
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000305}.
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DR   EMBL; CP000388; ABG40487.1; -; Genomic_DNA.
DR   RefSeq; WP_011574782.1; NC_008228.1.
DR   AlphaFoldDB; Q15UF1; -.
DR   SMR; Q15UF1; -.
DR   STRING; 342610.Patl_1969; -.
DR   EnsemblBacteria; ABG40487; ABG40487; Patl_1969.
DR   KEGG; pat:Patl_1969; -.
DR   eggNOG; COG0524; Bacteria.
DR   HOGENOM; CLU_027634_8_0_6; -.
DR   OMA; YWREQAP; -.
DR   OrthoDB; 1604782at2; -.
DR   BioCyc; MetaCyc:MON-19468; -.
DR   Proteomes; UP000001981; Chromosome.
DR   GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..318
FT                   /note="2-dehydro-3-deoxygluconokinase"
FT                   /id="PRO_0000449956"
FT   ACT_SITE        262
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         30..34
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         259..262
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ   SEQUENCE   318 AA;  35532 MW;  775BB1AE725D0BC5 CRC64;
     MRNPTFIAIG ECMVELSVTA QNKLQHSYAG DTYNSLVYAK RWHNELDCYF LSGIGQDSFS
     TLMTAHWQQH GISDEFALTS DDHNVGIYAI KNDDSGERHF DYWRKESAAT QLMSLIEQSD
     CESHWPHFDL VYFSGISLGI LSDEDKDKLI NLITRLKAKG SKVAFDPNYR PKMWANKAHA
     IRWLEAAYTV SDIVLPGTED HHDLLGHASV SEIVNYCKQY DVQELVVKAG KEGVFAFDCG
     QALCHVPFTP ADRQLDTTAA GDSFAGVYLA CRMADKPMKL SIEHASAAAG LVVQHQGAIV
     EHTIFDAFRQ RLANHTVA