ID   MAK_MYCSJ               Reviewed;         444 AA.
AC   A3Q7Y6;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=Mjls_5500;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) 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}.
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; CP000580; ABO01264.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3Q7Y6; -.
DR   SMR; A3Q7Y6; -.
DR   STRING; 164757.Mjls_5500; -.
DR   KEGG; mjl:Mjls_5500; -.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   BioCyc; MSP164757:G1G8C-5562-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_0000412890"
SQ   SEQUENCE   444 AA;  49435 MW;  AF817A239FF17765 CRC64;
     MNLPFDDWLP QQRWYGGRSR EFSSATADVV VTLRDDLDLV LLTVNYAEGR PEHYQILVRW
     DAAPIDEYSA 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