PPGK_MYCLE
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 03-AUG-2022, entry version 107.
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; Actinobacteria; Corynebacteriales; 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}.
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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.ML1023; -.
DR EnsemblBacteria; CAC31404; CAC31404; CAC31404.
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 OMA; HVEMLFS; -.
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 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; 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
