ID   MAK_MYCTF               Reviewed;         455 AA.
AC   A5WII2;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=TBFG_10128;
OS   Mycobacterium tuberculosis (strain F11).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=336982;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11;
RA   Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA   Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V.,
RA   Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S.,
RA   Shea T., Arachchi H., Macdonald P., Abouelleil A., Lui A., Priest M.,
RA   Berlin A., Gearin G., Brown A., Aftuck L., Bessette D., Allen N.,
RA   Lubonja R., Lokyitsang T., Matthews C., Dunbar C., Benamara M., Nguyen T.,
RA   Negash T., DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA   Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., O'Leary S.,
RA   Alvarado L., Victor T., Murray M.;
RT   "The complete genome sequence of Mycobacterium tuberculosis F11.";
RL   Submitted (APR-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}.
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DR   EMBL; CP000717; ABR04471.1; -; Genomic_DNA.
DR   RefSeq; WP_003899824.1; NZ_KK339377.1.
DR   AlphaFoldDB; A5WII2; -.
DR   SMR; A5WII2; -.
DR   KEGG; mtf:TBFG_10128; -.
DR   PATRIC; fig|336982.11.peg.146; -.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
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; 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_0000412897"
SQ   SEQUENCE   455 AA;  49889 MW;  FE561A06279FC6B9 CRC64;
     MTRSDTLATK LPWSDWLPRQ RWYAGRNREL ATVKPGVVVA LRHNLDLVLV DVTYTDGATE
     RYQVLVGWDF EPASEYGTKA AIGVADDRTG FDALYDVAGP QFLLSLIVSS AVCGTSTGEV
     TFTREPDVEL PFAAQPRVCD AEQSNTSVIF DRRAILKVFR RVSSGINPDI ELNRVLTRAG
     NPHVARLLGA YQFGRPNRSP TDALAYALGM VTEYEANAAE GWAMATASVR DLFAEGDLYA
     HEVGGDFAGE SYRLGEAVAS VHATLADSLG TAQATFPVDR MLARLSSTVA VVPELREYAP
     TIEQQFQKLA AEAITVQRVH GDLHLGQVLR TPESWLLIDF EGEPGQPLDE RRAPDSPLRD
     VAGVLRSFEY AAYGPLVDQA TDKQLAARAR EWVERNRAAF CDGYAVASGI DPRDSALLLG
     AYELDKAVYE TGYETRHRPG WLPIPLRSIA RLTAS