KDGK1_HALVD
ID KDGK1_HALVD Reviewed; 320 AA.
AC D4GSE6; L9UMS7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase {ECO:0000305};
DE Short=2-dehydro-3-deoxyglucono/galactono-kinase {ECO:0000305};
DE EC=2.7.1.178 {ECO:0000269|PubMed:25287957};
DE AltName: Full=2-keto-3-deoxygluconate/2-keto-3-deoxygalactonate kinase {ECO:0000305};
DE AltName: Full=KDG kinase {ECO:0000303|PubMed:25287957};
DE AltName: Full=KDGK-1 {ECO:0000303|PubMed:25287957};
GN Name=kdgK1 {ECO:0000303|PubMed:25287957};
GN OrderedLocusNames=HVO_0549 {ECO:0000312|EMBL:ADE04815.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DS2 / DS70 / H26;
RX PubMed=25287957; DOI=10.1111/1574-6968.12617;
RA Pickl A., Johnsen U., Archer R.M., Schoenheit P.;
RT "Identification and characterization of 2-keto-3-deoxygluconate kinase and
RT 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii.";
RL FEMS Microbiol. Lett. 361:76-83(2014).
CC -!- FUNCTION: Involved in the degradation of glucose via the semi-
CC phosphorylative Entner-Doudoroff pathway. Catalyzes the phosphorylation
CC of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-
CC phosphogluconate (KDPG). Also catalyzes efficiently the phosphorylation
CC of 2-keto-3-deoxygalactonate (KDGal) to 2-keto-3-deoxy-6-
CC phosphogalactonate (KDPGal). {ECO:0000269|PubMed:25287957}.
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=2.7.1.178;
CC Evidence={ECO:0000269|PubMed:25287957};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14798;
CC Evidence={ECO:0000269|PubMed:25287957};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-dehydro-3-deoxy-D-galactonate + ATP = 2-dehydro-3-deoxy-6-
CC phospho-D-galactonate + ADP + H(+); Xref=Rhea:RHEA:16525,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57989,
CC ChEBI:CHEBI:58298, ChEBI:CHEBI:456216; EC=2.7.1.178;
CC Evidence={ECO:0000269|PubMed:25287957};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16526;
CC Evidence={ECO:0000269|PubMed:25287957};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.54 mM for KDG {ECO:0000269|PubMed:25287957};
CC KM=0.73 mM for KDGal {ECO:0000269|PubMed:25287957};
CC KM=0.36 mM for ATP {ECO:0000269|PubMed:25287957};
CC Vmax=78 umol/min/mg enzyme with KDG as substrate
CC {ECO:0000269|PubMed:25287957};
CC Vmax=33 umol/min/mg enzyme with KDGal as substrate
CC {ECO:0000269|PubMed:25287957};
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. {ECO:0000305}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:25287957}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:25287957}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes growth on glucose,
CC but does not affect growth on galactose. Double deletion mutant
CC kdgK1/kdgK2 loses the ability to grow on galactose.
CC {ECO:0000269|PubMed:25287957}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; CP001956; ADE04815.1; -; Genomic_DNA.
DR RefSeq; WP_004044382.1; NZ_AOHU01000099.1.
DR AlphaFoldDB; D4GSE6; -.
DR SMR; D4GSE6; -.
DR STRING; 309800.C498_15984; -.
DR EnsemblBacteria; ADE04815; ADE04815; HVO_0549.
DR GeneID; 8924883; -.
DR KEGG; hvo:HVO_0549; -.
DR PATRIC; fig|309800.29.peg.3092; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_0_1_2; -.
DR OMA; MAMFYAN; -.
DR OrthoDB; 36944at2157; -.
DR BRENDA; 2.7.1.178; 2561.
DR BRENDA; 2.7.1.45; 2561.
DR UniPathway; UPA00856; UER00828.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0008671; F:2-dehydro-3-deoxygalactonokinase activity; IEA:RHEA.
DR GO; GO:0008673; F:2-dehydro-3-deoxygluconokinase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
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..320
FT /note="2-dehydro-3-deoxygluconokinase/2-dehydro-3-
FT deoxygalactonokinase"
FT /id="PRO_0000449269"
FT ACT_SITE 262
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 34..38
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 107..109
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 169..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 230..235
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"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ SEQUENCE 320 AA; 34083 MW; 98EB5BCFE982A17A CRC64;
MTALVTFGET MLRLSPPRGE RLETARELEV QAGGAESNVA VAAARLGRDA AWFSKLPDSP
LGRRIVSELR SHSVDTDGVV WTDDADARQG VYYLEHGASP RPTNVVYDRA DAAVTTLETG
EFDLDAVRDA EVCFTSGITP ALSETLSETT ADVLDEAQNA GTTTAFDLNY RTKLWSPDEA
AEVYRDLLDS VDLLFAAERD AATVLGRDGD AESVARGLAD DYDIETVVVT RGEEGSLAVS
DGAVSEQGVY ETETYDAIGT GDAFVGGFLA KHLDGGSVTE SLEWASATAS FKRTVEGDIA
VVTPEDVERV VAEEGDGISR
