ID   PPGK_MYCTO              Reviewed;         265 AA.
AC   P9WIN0; 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 37.
DE   RecName: Full=Polyphosphate glucokinase;
DE            EC=2.7.1.63;
DE   AltName: Full=ATP-dependent glucokinase;
DE            EC=2.7.1.2;
DE   AltName: Full=Polyphosphate--glucose phosphotransferase;
GN   Name=ppgK; OrderedLocusNames=MT2776;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate
CC       or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems
CC       to be the major phosphate donor for the enzyme in M.tuberculosis.
CC       {ECO:0000250|UniProtKB:A5U654}.
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:0000250|UniProtKB:A5U654};
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:0000250|UniProtKB:A5U654};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A5U654}.
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; AE000516; AAK47091.1; -; Genomic_DNA.
DR   PIR; A70531; A70531.
DR   RefSeq; WP_003899438.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIN0; -.
DR   SMR; P9WIN0; -.
DR   EnsemblBacteria; AAK47091; AAK47091; MT2776.
DR   KEGG; mtc:MT2776; -.
DR   PATRIC; fig|83331.31.peg.2989; -.
DR   HOGENOM; CLU_065796_0_0_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..265
FT                   /note="Polyphosphate glucokinase"
FT                   /id="PRO_0000427977"
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"
SQ   SEQUENCE   265 AA;  27390 MW;  2F5B1B1B5C30ECE5 CRC64;
     MTSTGPETSE TPGATTQRHG FGIDVGGSGI KGGIVDLDTG QLIGDRIKLL TPQPATPLAV
     AKTIAEVVNG FGWRGPLGVT YPGVVTHGVV RTAANVDKSW IGTNARDTIG AELGGQQVTI
     LNDADAAGLA ETRYGAGKNS PGLVVLLTFG TGIGSAVIHN GTLIPNTEFG HLEVGGKEAE
     ERAASSVKEK NDWTYPKWAK QVTRVLIAIE NAIWPDLFIA GGGISRKADK WVPLLENRTP
     VVPAALQNTA GIVGAAMASV ADTTH