ID   PPGK_MYCLE              Reviewed;         324 AA.
AC   Q49988;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=ML1023; ORFNames=u1764fg;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Catalyzes the phosphorylation of glucose using polyphosphate
CC       or ATP as the phosphoryl donor. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U15181; AAA62940.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31404.1; -; Genomic_DNA.
DR   PIR; A87037; A87037.
DR   RefSeq; NP_301756.1; NC_002677.1.
DR   AlphaFoldDB; Q49988; -.
DR   SMR; Q49988; -.
DR   STRING; 272631.gene:17574849; -.
DR   KEGG; mle:ML1023; -.
DR   PATRIC; fig|272631.5.peg.1852; -.
DR   Leproma; ML1023; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_065796_0_0_11; -.
DR   OrthoDB; 849313at2; -.
DR   Proteomes; UP000000806; 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   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000600; ROK.
DR   PANTHER; PTHR18964:SF146; POLYPHOSPHATE GLUCOKINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..324
FT                   /note="Polyphosphate glucokinase"
FT                   /id="PRO_0000058535"
FT   REGION          53..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..88
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   324 AA;  34102 MW;  563A5C63CC9EF6EA CRC64;
     MIRLRSAAAR DRCQVLSLAY RITVAGRCQT VSPHHRQAKV SEQPSLAKEI AITSTDATAD
     TPRTSPPSDT AGTTSRHRGF GIDIGGSSIK GGIVDLDIGQ LIGDRIKLLT PQPATPLAVA
     KTIAEVVNAF GWTAPLGVTY PGVVTQGVVR TAANVDDSWI GTNARDIISA ELNSQEVTIL
     NDADAAGLAE GRYGAGKNNS GLIVLLTFGT GIGSAVIHNG KLIPNTEFGH LEVDGKEAEQ
     RAASSVKDKY KWSYRTWAKQ VTRVLVAIEN AMCPDLFIAG GGISRKADRW IPLLENRTPM
     VAAALQNTAG IVGAAMASTA DVTH
//