ID   MAK_MYCTA               Reviewed;         455 AA.
AC   A5TYK2;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=MRA_0134;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ71852.1; -; Genomic_DNA.
DR   RefSeq; WP_003916610.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5TYK2; -.
DR   SMR; A5TYK2; -.
DR   STRING; 419947.MRA_0134; -.
DR   EnsemblBacteria; ABQ71852; ABQ71852; MRA_0134.
DR   KEGG; mra:MRA_0134; -.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   OrthoDB; 268166at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001988; 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_0000412896"
SQ   SEQUENCE   455 AA;  49879 MW;  7D643689E94F5ED4 CRC64;
     MTRSDTLATK LPWSDWLSRQ 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