ID   MAK_MYCGI               Reviewed;         430 AA.
AC   A4T432;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; OrderedLocusNames=Mflv_1087;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
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; CP000656; ABP43569.1; -; Genomic_DNA.
DR   RefSeq; WP_011891986.1; NC_009338.1.
DR   AlphaFoldDB; A4T432; -.
DR   SMR; A4T432; -.
DR   STRING; 350054.Mflv_1087; -.
DR   EnsemblBacteria; ABP43569; ABP43569; Mflv_1087.
DR   KEGG; mgi:Mflv_1087; -.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_029675_0_0_11; -.
DR   OMA; TAFCDGY; -.
DR   OrthoDB; 268166at2; -.
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; 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_0000412886"
SQ   SEQUENCE   430 AA;  46834 MW;  8633AE36B995E863 CRC64;
     MTLAFGEWII HRRWYAGRTR ELASAQPAAV TALGDGLDHV LLDVAYTDGF TERYQILVQW
     ESAPVDRYGE AALIGTSSGP DGTRFAYDAL FNPEAASRLL RLINSSETVG ELTFSREPDV
     TLPVDAPAKV SGAEQSNTSV IFGKDAMLKV FRRVTPGINP DIELNRVLAR AGNPRVATLL
     GSFETSSCAL GMVTAFAANS AEGWDMATAS VHDLFANEVG GDFADESRRL GEAVASVHAT
     LAGALGTSVA EFPIDTVLDR LRVATQAAPE LAPYAPRIEE RFRRLAERPI QVHRVHGDLH
     LGQVLRTPES WLLIDFEGEP GQPLEDRRRP DSPLRDVAGV LRSFEYAAYQ QVVTGGGDAQ
     MAERARSWVD RNVDAFCAGY AAVAGEDPRA SGDVLAAYEL DKAVYEAAYE ARFRPSWLPI
     PMRSIQRLVS