ID   MAK_MYCSR               Reviewed;         430 AA.
AC   E6TMM3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=Mspyr1_51010;
OS   Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS   (Mycobacterium gilvum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=278137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA   Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL   Submitted (DEC-2010) 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; CP002385; ADU01629.1; -; Genomic_DNA.
DR   RefSeq; WP_013473105.1; NC_014814.1.
DR   AlphaFoldDB; E6TMM3; -.
DR   SMR; E6TMM3; -.
DR   EnsemblBacteria; ADU01629; ADU01629; Mspyr1_51010.
DR   KEGG; msp:Mspyr1_51010; -.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008916; 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; 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..430
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412893"
SQ   SEQUENCE   430 AA;  46646 MW;  375CC9382514B6AC CRC64;
     MTLAFGEWII HRRWYAGRTR ELASVEPAAV TALGGGLDHV LLDVAYTDGS TERYQVLVQW
     ESEPVDGYGE AALIGTASGP DGTRVAYDAL FNPEAAGRLL SLINRSETIG ELTFSREPDV
     TLPVDAPAKV SGAEQSNTSV IFGKDAMLKV FRRVTPGVNP DIELNRVLAR AGNPHVATLL
     GAFETSSCAL GMVTAFAANS AEGWDMATAS VHDLFANEVG GDFADESRRL GAAVASVHAT
     LADTLGTSVT QFPIDTVLER LRSATRAAPE LAPYAPQIEQ RFRRLADQPI RVHRIHGDLH
     LGQVLRTPES WLLIDFEGEP GQPLEERRRP DSPLRDVAGV LRSFEYAAYQ QVVTGGGDPQ
     MADRARSWVD RNVDAFCAGY AAVAGEDPRA SGDVLAAYEL DKAVYEAAYE ARFRPSWLPI
     PMRSIQRLVS