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   16-JUN-2009, entry version 51.
DE   RecName: Full=Polyphosphate glucokinase;
DE            EC=2.7.1.63;
DE   AltName: Full=Polyphosphate--glucose phosphotransferase;
GN   Name=ppgK; OrderedLocusNames=ML1023; ORFNames=u1764fg;
OS   Mycobacterium leprae.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1769;
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   MEDLINE=21128732; 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
CC       polyphosphate or ATP as the phosphoryl donor.
CC   -!- CATALYTIC ACTIVITY: (Phosphate)(n) + D-glucose = (phosphate)(n-1)
CC       + D-glucose 6-phosphate.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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; -.
DR   GeneID; 910085; -.
DR   GenomeReviews; AL450380_GR; ML1023.
DR   KEGG; mle:ML1023; -.
DR   NMPDR; fig|272631.1.peg.628; -.
DR   Leproma; ML1023; -.
DR   HOGENOM; Q49988; -.
DR   OMA; Q49988; WEKWAKR.
DR   BioCyc; MLEP272631:ML1023-MON; -.
DR   BRENDA; 2.7.1.63; 808.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047330; F:polyphosphate-glucose phosphotransferase ac...; IEA:EC.
DR   InterPro; IPR000600; ROK.
DR   Pfam; PF00480; ROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    324       Polyphosphate glucokinase.
FT                                /FTId=PRO_0000058535.
FT   NP_BIND      83     88       ATP (Potential).
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
//