ID   MAK_MYCUA               Reviewed;         455 AA.
AC   A0PWI9;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=MUL_4796;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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; CP000325; ABL06708.1; -; Genomic_DNA.
DR   RefSeq; WP_011742300.1; NC_008611.1.
DR   AlphaFoldDB; A0PWI9; -.
DR   SMR; A0PWI9; -.
DR   STRING; 362242.MUL_4796; -.
DR   EnsemblBacteria; ABL06708; ABL06708; MUL_4796.
DR   KEGG; mul:MUL_4796; -.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000765; Chromosome.
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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR040999; Mak_N_cap.
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..455
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412899"
SQ   SEQUENCE   455 AA;  49355 MW;  922EE3FCE1A845F7 CRC64;
     MNSPATLAAK LPWSEWLPQQ RWYAGRNREL AAAEPGAVVA LRDDLDLVLV DVSYTDGSAE
     RYQVLVRWDA GPVSEFSTLA TIGSADDHTG FDALYDPVAP QVLLSLIDSS AVRSSSDGQV
     SFAREPDVEL PLDAYPRVSD AEQSNTSVIF DRGQAAILKV FRRVSSGINP DIELNRVLGR
     AHNPHVARLL GTYEIGIPGE PPEAACPLGM ATAYAANAAE GWAMATASVR DLFAEGDLYA
     HEVGGDFAGE SRRLGEAVAS VHATLAEQLG TAQATFPVDH VLARLSSTAA AVPELQQYAG
     TIEERFVKLV DETISVQRVH GDLHLGQVLR TPESWVLIDF EGESGQPLRE RRAPDSPLRD
     VAGVLRSFEY AAYGPLVDHA DDKQLAARAR EWITRNRTAF CEGYAAASGN DPRDSELLLA
     AYELDKAVYE AGYESRHRPG WLPIPLRSIA RLTAT