ID   MAK_ACTMI               Reviewed;         437 AA.
AC   Q7WUM3;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak1;
OS   Actinoplanes missouriensis.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=1866;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15378530; DOI=10.1002/jobm.200410403;
RA   Jarling M., Cauvet T., Grundmeier M., Kuhnert K., Pape H.;
RT   "Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2
RT   from Streptomyces coelicolor is a maltokinase.";
RL   J. Basic Microbiol. 44:360-373(2004).
RN   [2]
RP   FUNCTION AS A MALTOKINASE, AND CATALYTIC ACTIVITY.
RX   PubMed=8690081; DOI=10.1016/0014-5793(96)00554-6;
RA   Drepper A., Peitzmann R., Pape H.;
RT   "Maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes sp.:
RT   demonstration of enzyme activity and characterization of the reaction
RT   product.";
RL   FEBS Lett. 388:177-179(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-25, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=12879214; DOI=10.1007/s00203-003-0575-y;
RA   Niehues B., Jossek R., Kramer U., Koch A., Jarling M., Schroder W.,
RA   Pape H.;
RT   "Isolation and characterization of maltokinase (ATP:maltose 1-
RT   phosphotransferase) from Actinoplanes missouriensis.";
RL   Arch. Microbiol. 180:233-239(2003).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of maltose to
CC       maltose 1-phosphate. Only maltose acts effectively as phosphoryl-group
CC       acceptor, but maltotriose, maltotetraose, maltopentaose, and
CC       maltohexaose show a weak potential to replace maltose. ATP is not
CC       replaceable as phosphoryl-group donor. {ECO:0000269|PubMed:8690081}.
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; Evidence={ECO:0000269|PubMed:8690081};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:12879214}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.6 mM for maltose (at pH 8) {ECO:0000269|PubMed:12879214};
CC         KM=0.54 mM for ATP (at pH 8) {ECO:0000269|PubMed:12879214};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:12879214};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius. The enzyme activity
CC         decreases rapidly at temperatures above 60 degrees Celsius.
CC         {ECO:0000269|PubMed:12879214};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12879214}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000305}.
CC   -!- MISCELLANEOUS: In the presence of 20 mM MgCl(2), the addition of
CC       CaCl(2), CoCl(2), FeSO(4), MnCl(2), BaCl(2) or CuCl(2) at a
CC       concentration of 1 mM to the enzyme assay led to a decrease of activity
CC       between 20% (FeSO(4)) and 83% (CoCl(2)).
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AY327498; AAQ01690.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7WUM3; -.
DR   SMR; Q7WUM3; -.
DR   BRENDA; 2.7.1.175; 141.
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; IDA:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IDA: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   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycogen biosynthesis; Glycogen metabolism; Kinase; Nucleotide-binding;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12879214"
FT   CHAIN           2..437
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412881"
SQ   SEQUENCE   437 AA;  47731 MW;  BBB0B056BCEE9936 CRC64;
     MTLPFAEWLP KQRWYAGRSR VLASVKEASA TPLGEELDLV LVDVEYTDGS SERYQVMVGW
     GDGPLPEYST IASIGTADDG RDGYDALYDP RATRHLLGLV DTSATAGDVT FEKEPGVELP
     LEAWPRVFDA EQSNTSVIFD EDAILKLFRR VTCGVNPDIE LNRVLGRAGN PHVARLLGSL
     QSADDSGPCS LGMVTEYAAN SAEGWAMATA SARDLFADAE MRADEVGGDF QGESYRLGEA
     VASVHRTLAE ELGTGPAPFP LDAVLARVRT AAAAVPELQQ FVPAITARFE ALTGAEVVVQ
     RVHGDLHLGQ VLRTPEAWLL IDFEGEPGQP LDERRMPDSP LRDVAGVLRS YEYAAYQLLV
     DQDDDEHLAA RAREWVDRNR AAFCDGYTNV AGADPREQGA LLSAYELDKA VYEAAYEARH
     RPGWLRIPLR SITRLVG