KDGK2_HALVD
ID KDGK2_HALVD Reviewed; 318 AA.
AC D4GR05; L9V354;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=2-dehydro-3-deoxygalactonokinase {ECO:0000305};
DE EC=2.7.1.58 {ECO:0000269|PubMed:25287957};
DE AltName: Full=2-keto-3-deoxygalactonate kinase {ECO:0000303|PubMed:25287957};
DE Short=KDGal kinase {ECO:0000303|PubMed:25287957};
DE AltName: Full=KDGK-2 {ECO:0000303|PubMed:25287957};
GN Name=kdgK2 {ECO:0000303|PubMed:25287957};
GN OrderedLocusNames=HVO_A0328 {ECO:0000312|EMBL:ADE02032.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4.
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 galactose catabolism. Catalyzes the
CC phosphorylation of 2-keto-3-deoxygalactonate (KDGal) to produce 2-keto-
CC 3-deoxy-6-phosphogalactonate (KDPGal). Can also phosphorylate 2-keto-3-
CC deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDPG), but
CC the catalytic efficiency for KDGal is 50-fold higher than for KDG.
CC {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=2.7.1.58;
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=0.2 mM for KDGal {ECO:0000269|PubMed:25287957};
CC KM=8.8 mM for KDG {ECO:0000269|PubMed:25287957};
CC KM=0.3 mM for ATP {ECO:0000269|PubMed:25287957};
CC Vmax=148 umol/min/mg enzyme with KDGal as substrate
CC {ECO:0000269|PubMed:25287957};
CC Vmax=125 umol/min/mg enzyme with KDG as substrate
CC {ECO:0000269|PubMed:25287957};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:25287957}.
CC -!- INDUCTION: Highly induced by galactose. {ECO:0000269|PubMed:25287957}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not affect growth on
CC glucose or galactose. Double deletion mutant kdgK1/kdgK2 loses the
CC ability to grow on galactose. {ECO:0000269|PubMed:25287957}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; CP001955; ADE02032.1; -; Genomic_DNA.
DR RefSeq; WP_004043241.1; NZ_AOHU01000058.1.
DR AlphaFoldDB; D4GR05; -.
DR SMR; D4GR05; -.
DR STRING; 309800.C498_10271; -.
DR EnsemblBacteria; ADE02032; ADE02032; HVO_A0328.
DR GeneID; 8923588; -.
DR KEGG; hvo:HVO_A0328; -.
DR PATRIC; fig|309800.29.peg.1997; -.
DR eggNOG; arCOG00014; Archaea.
DR HOGENOM; CLU_027634_0_1_2; -.
DR OMA; CIGIEPL; -.
DR OrthoDB; 36944at2157; -.
DR BRENDA; 2.7.1.11; 2561.
DR BRENDA; 2.7.1.178; 2561.
DR BRENDA; 2.7.1.58; 2561.
DR Proteomes; UP000008243; Plasmid pHV4.
DR GO; GO:0008671; F:2-dehydro-3-deoxygalactonokinase 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; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..318
FT /note="2-dehydro-3-deoxygalactonokinase"
FT /id="PRO_0000449270"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 35..39
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 105..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 167..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 169
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 257..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q97U29"
SQ SEQUENCE 318 AA; 33998 MW; 98998ACAD21E1BA2 CRC64;
MTAELVTFGE TMIRLSPPEG ERIETARSLE FRTAGAESNV AVAASRLGCS AAWLSKLPDS
PLGRRVTTEL RTHGVEPYVR WDDDARQGAY YIEQGRAPRP TNVIYDRADA AVTTARPDEL
AVDIVEDAAA FYTSGITPAL SETLRETTGE LLQTATEAGT TTAFDLNYRS KLWSPSDARD
ACESLFPKVD VLVAAERDIR AVLELDGDAP TLASELAGDF DFETVVVTRG EDGALARHGG
TVYEQPVFET DTVDAIGTGD AFVGAFLSRL IAGEPVETAL AYGAATAALK RTVHGDLAVV
TPDEVERVLR GGDAGIDR
