PPGK_MYCTA
ID PPGK_MYCTA Reviewed; 265 AA.
AC A5U654;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Polyphosphate glucokinase {ECO:0000303|PubMed:8381043};
DE Short=Poly(P) glucokinase {ECO:0000303|PubMed:8381043};
DE EC=2.7.1.63 {ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950};
DE AltName: Full=ATP-dependent glucokinase {ECO:0000303|PubMed:8381043};
DE EC=2.7.1.2 {ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950};
DE AltName: Full=Polyphosphate--glucose phosphotransferase;
GN Name=ppgK; OrderedLocusNames=MRA_2730;
OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=419947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA Wang H., Wang S., Zhao G., Zhang Y.;
RT "Genetic basis of virulence attenuation revealed by comparative genomic
RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL PLoS ONE 3:E2375-E2375(2008).
RN [2]
RP PROTEIN SEQUENCE OF 19-42; 120-138 AND 169-178.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=8617763; DOI=10.1074/jbc.271.9.4909;
RA Hsieh P.-C., Shenoy B.C., Samols D., Phillips N.F.B.;
RT "Cloning, expression, and characterization of polyphosphate glucokinase
RT from Mycobacterium tuberculosis.";
RL J. Biol. Chem. 271:4909-4915(1996).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=8381043; DOI=10.1006/prep.1993.1012;
RA Hsieh P.C., Shenoy B.C., Jentoft J.E., Phillips N.F.;
RT "Purification of polyphosphate and ATP glucose phosphotransferase from
RT Mycobacterium tuberculosis H37Ra: evidence that poly(P) and ATP glucokinase
RT activities are catalyzed by the same enzyme.";
RL Protein Expr. Purif. 4:76-84(1993).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION
RP MECHANISM.
RC STRAIN=ATCC 25177 / H37Ra;
RX PubMed=8703950; DOI=10.1021/bi9528659;
RA Hsieh P.C., Kowalczyk T.H., Phillips N.F.;
RT "Kinetic mechanisms of polyphosphate glucokinase from Mycobacterium
RT tuberculosis.";
RL Biochemistry 35:9772-9781(1996).
CC -!- FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate
CC or ATP as the phosphoryl donor (PubMed:8381043, PubMed:8703950).
CC Polyphosphate, rather than ATP, seems to be the major phosphate donor
CC for the enzyme in M.tuberculosis (PubMed:8703950). GTP, UTP and CTP can
CC replace ATP as phosphoryl donor (PubMed:8381043).
CC {ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-
CC phosphate + H(+); Xref=Rhea:RHEA:22036, Rhea:RHEA-COMP:9859,
CC Rhea:RHEA-COMP:14279, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16838, ChEBI:CHEBI:61548; EC=2.7.1.63;
CC Evidence={ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC Evidence={ECO:0000269|PubMed:8381043, ECO:0000269|PubMed:8703950};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.4 uM for (Phosphate)(32) (at pH 8.6)
CC {ECO:0000269|PubMed:8381043};
CC KM=13.9 uM for polyphosphate type 35 (Sigma) (at pH 7.5)
CC {ECO:0000269|PubMed:8703950};
CC KM=6.1 uM for polyphosphate type 35 (Sigma) (at pH 8.6)
CC {ECO:0000269|PubMed:8703950};
CC KM=0.28 mM for D-glucose (at pH 7.5, in the polyphosphate-dependent
CC glucokinase reaction) {ECO:0000269|PubMed:8703950};
CC KM=0.37 mM for D-glucose (at pH 8.6, in the polyphosphate-dependent
CC glucokinase reaction) {ECO:0000269|PubMed:8703950};
CC KM=0.06 mM for D-glucose (at pH 7.5, in the ATP-dependent glucokinase
CC reaction) {ECO:0000269|PubMed:8703950};
CC KM=0.22 mM for D-glucose (at pH 8.6, in the ATP-dependent glucokinase
CC reaction) {ECO:0000269|PubMed:8703950};
CC KM=0.88 mM for ATP (at pH 7.5) {ECO:0000269|PubMed:8703950};
CC KM=1.4 mM for ATP (at pH 8.6) {ECO:0000269|PubMed:8703950};
CC KM=1.46 mM for ATP (at pH 8.6) {ECO:0000269|PubMed:8381043};
CC KM=0.29 mM for GTP (at pH 8.6) {ECO:0000269|PubMed:8381043};
CC KM=1.43 mM for dATP (at pH 8.6) {ECO:0000269|PubMed:8381043};
CC KM=2.19 mM for UTP (at pH 8.6) {ECO:0000269|PubMed:8381043};
CC KM=8.32 mM for CTP (at pH 8.6) {ECO:0000269|PubMed:8381043};
CC Note=kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as
CC substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35
CC (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as
CC substrate at pH 7.5. kcat is 116 sec(-1) with ATP as substrate at pH
CC 8.6 (PubMed:8703950). kcat is 149 sec(-1) with poly(P)(32) as
CC substrate at pH 8.6. kcat is 60 sec(-1) with ATP as substrate at pH
CC 8.6. kcat is 60 sec(-1) with GTP as substrate at pH 8.6. kcat is 61
CC sec(-1) with dATP as substrate at pH 8.6. kcat is 37 sec(-1) with UTP
CC as substrate at pH 8.6. kcat is 19 sec(-1) with CTP as substrate at
CC pH 8.6 (PubMed:8381043). {ECO:0000269|PubMed:8381043,
CC ECO:0000269|PubMed:8703950};
CC pH dependence:
CC Optimum pH is 9.5 and 9.6-9.5 with poly(P)(32) and ATP as the
CC phosphoryl donors, respectively. {ECO:0000269|PubMed:8381043};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius for both activities.
CC {ECO:0000269|PubMed:8381043};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8381043}.
CC -!- MISCELLANEOUS: The poly(P)- and ATP-dependent glucokinase reactions
CC both follow an ordered Bi-Bi mechanism, with glucose being the second
CC substrate to bind and glucose 6-phosphate being released last. The
CC mechanism of poly(P) utilization is not strictly processive and is most
CC likely nonprocessive, where there is dissociation of poly(P) prior to
CC complete utilization. {ECO:0000269|PubMed:8703950}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; CP000611; ABQ74504.1; -; Genomic_DNA.
DR RefSeq; WP_003911949.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U654; -.
DR SMR; A5U654; -.
DR STRING; 419947.MRA_2730; -.
DR EnsemblBacteria; ABQ74504; ABQ74504; MRA_2730.
DR KEGG; mra:MRA_2730; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_065796_0_0_11; -.
DR OMA; HVEMLFS; -.
DR OrthoDB; 1130699at2; -.
DR SABIO-RK; A5U654; -.
DR Proteomes; UP000001988; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0047330; F:polyphosphate-glucose phosphotransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..265
FT /note="Polyphosphate glucokinase"
FT /id="PRO_0000306419"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 19
FT /note="H -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="T -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..42
FT /note="QL -> EI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 132..133
FT /note="TR -> EH (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 173..175
FT /note="EVG -> QDV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 265 AA; 27429 MW; 2F4AFAFAAC3C01E5 CRC64;
MTSTGPETSE TPGATTQRHG FGIDVGGSGI KGGIVDLDTG QLIGDRIKLL TPQPATPLAV
AKTIAEVVNG FGWRGPLGVT YPGVVTHGVV RTAANVDKSW IGTNARDTIG AELGGQQVTI
LNDADAAGLA ETRYGAGKNN PGLVVLLTFG TGIGSAVIHN GTLIPNTEFG HLEVGGKEAE
ERAASSVKEK NDWTYPKWAK QVIRVLIAIE NAIWPDLFIA GGGISRKADK WVPLLENRTP
VVPAALQNTA GIVGAAMASV ADTTH
