ID   MAK_MYCPA               Reviewed;         452 AA.
AC   Q73U39;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=MAP_3529;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS06079.1; -; Genomic_DNA.
DR   RefSeq; WP_003879051.1; NC_002944.2.
DR   AlphaFoldDB; Q73U39; -.
DR   SMR; Q73U39; -.
DR   STRING; 262316.MAP_3529; -.
DR   EnsemblBacteria; AAS06079; AAS06079; MAP_3529.
DR   KEGG; mpa:MAP_3529; -.
DR   PATRIC; fig|262316.17.peg.3757; -.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000580; 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; Reference proteome;
KW   Transferase.
FT   CHAIN           1..452
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412888"
SQ   SEQUENCE   452 AA;  49210 MW;  38D12EE7EB3F2C6B CRC64;
     MTEPAKLPWS DWLPQQRWYA GRNRRLTGAE PSVIVGLRDD LDLVLVDADY ADGSRDRYQV
     LVRWDAAPVS EYSTVATIGA ADDRTGFDAL YDDEAPQFLL SLIDSSAVRS ASGAEVRFAK
     EPDAQLPLEA MAHVSDAEQS NTSVIFDRDA IFKVFRRVSS GINPDIELNR VLGRAGNPHV
     ARLLGTYEMA GADGTPETAW PLGMVTEFAA NAAEGWAMAT ASVRDLFAEG DLYAHEVGGD
     FAGESYRLGE AVASVHATLA ETLGTSQAAF PVDNVLARLS STAALVPELT EYAATIEERF
     AKLATETITV QRVHGDLHLG QVLRTPESWL LIDFEGEPGQ PLEERRAPDS PLRDVAGVLR
     SFEYAAYGPL VEQGAQNTDK QLAARAREWV ERNRTAFCDG YAAASGIDPR DSAPLLAAYE
     LDKAVYEAGY EARHRPGWLP IPLRSIARLT TA