PPGK_MYCTU
ID PPGK_MYCTU Reviewed; 265 AA.
AC P9WIN1; L0TAD9; O07204; Q59568;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Polyphosphate glucokinase {ECO:0000303|PubMed:8617763};
DE Short=Poly(P) glucokinase {ECO:0000303|PubMed:8617763};
DE EC=2.7.1.63 {ECO:0000269|PubMed:8617763};
DE AltName: Full=ATP-dependent glucokinase {ECO:0000303|PubMed:8617763};
DE EC=2.7.1.2 {ECO:0000269|PubMed:8617763};
DE AltName: Full=Polyphosphate--glucose phosphotransferase;
GN Name=ppgK {ECO:0000303|PubMed:8617763}; OrderedLocusNames=Rv2702;
GN ORFNames=MTCY05A6.23;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate
CC or ATP as the phosphoryl donor (PubMed:8617763). Polyphosphate, rather
CC than ATP, seems to be the major phosphate donor for the enzyme in
CC M.tuberculosis (By similarity). {ECO:0000250|UniProtKB:A5U654,
CC ECO:0000269|PubMed:8617763}.
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:8617763};
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:8617763};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A5U654}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000305|PubMed:19099550}.
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:0000250|UniProtKB:A5U654}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; U44834; AAC43638.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45500.1; -; Genomic_DNA.
DR PIR; A70531; A70531.
DR RefSeq; NP_217218.1; NC_000962.3.
DR RefSeq; WP_003911949.1; NZ_NVQJ01000017.1.
DR AlphaFoldDB; P9WIN1; -.
DR SMR; P9WIN1; -.
DR STRING; 83332.Rv2702; -.
DR PaxDb; P9WIN1; -.
DR DNASU; 887313; -.
DR GeneID; 887313; -.
DR KEGG; mtu:Rv2702; -.
DR TubercuList; Rv2702; -.
DR eggNOG; COG1940; Bacteria.
DR OMA; HVEMLFS; -.
DR PhylomeDB; P9WIN1; -.
DR BioCyc; MetaCyc:G185E-6950-MON; -.
DR BRENDA; 2.7.1.63; 3445.
DR PHI-base; PHI:3636; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IDA:MTBBASE.
DR GO; GO:0047330; F:polyphosphate-glucose phosphotransferase activity; IDA:MTBBASE.
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; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..265
FT /note="Polyphosphate glucokinase"
FT /id="PRO_0000058536"
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 203
FT /note="I -> T (in Ref. 1; AAC43638)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="R -> C (in Ref. 1; AAC43638)"
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
