ID   MAK_MYCSS               Reviewed;         444 AA.
AC   Q1B1L0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=Mmcs_5120;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of maltose to
CC       maltose 1-phosphate. Is involved in a branched alpha-glucan
CC       biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-maltose = ADP + alpha-maltose 1-phosphate + H(+);
CC         Xref=Rhea:RHEA:31915, ChEBI:CHEBI:15378, ChEBI:CHEBI:17306,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:63576, ChEBI:CHEBI:456216;
CC         EC=2.7.1.175;
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000384; ABG11224.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1B1L0; -.
DR   SMR; Q1B1L0; -.
DR   KEGG; mmc:Mmcs_5120; -.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   BioCyc; MSP164756:G1G6O-5234-MON; -.
DR   UniPathway; UPA00164; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005992; P:trehalose biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR040999; Mak_N_cap.
DR   Pfam; PF01636; APH; 1.
DR   Pfam; PF18085; Mak_N_cap; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN           1..444
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412892"
SQ   SEQUENCE   444 AA;  49489 MW;  F9EE200E82A8300F CRC64;
     MNLPFDDWLP QQRWYGGRSR EFSSATPDVV VTLRDDLDLV LLTVNYAEGR PEHYQILVRW
     DAAPIDEYSV VARIGSDTEH GERTGYDALY DPAAAHFLMT LIDSSAQVGD IRFAKEPEVT
     LPLQAAPRVS SAEQSNTSVI FDQDAILKVF RRITPGINPD IELNRVLARA GNPHVARLLG
     SFETTLDREP YALGMVTEFA ANSAEGWDMA LTSTRDLFAE GDLYADEVGG DFAGESHRLG
     EAVASVHSTL AAELGTSQVP FPLDTVLERL QSVADAVPEL QPHAQSIEER YRKLADQEIT
     VHRVHGDLHL GQVLRTTEGW LLIDFEGEPG QPLDERRRPD SPMRDVAGML RSYEYAAYQR
     LIERGGDAQH DKQLAARARE WVNRNVSSFC DGYAAASGTD PRDHAELLAA YELDKAVYEV
     GYEARYRPSW LPIPMKSILR ILGV