ID   MAK_MYCS2               Reviewed;         441 AA.
AC   A0R6D9; I7FV18;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Maltokinase;
DE            Short=MaK;
DE            EC=2.7.1.175;
DE   AltName: Full=Maltose-1-phosphate synthase;
GN   Name=mak; Synonyms=pep2; OrderedLocusNames=MSMEG_6514, MSMEI_6342;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=20305657; DOI=10.1038/nchembio.340;
RA   Kalscheuer R., Syson K., Veeraraghavan U., Weinrick B., Biermann K.E.,
RA   Liu Z., Sacchettini J.C., Besra G., Bornemann S., Jacobs W.R. Jr.;
RT   "Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an
RT   alpha-glucan pathway.";
RL   Nat. Chem. Biol. 6:376-384(2010).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of maltose to
CC       maltose 1-phosphate (Probable). Is involved in a branched alpha-glucan
CC       biosynthetic pathway from trehalose, together with TreS, GlgE and GlgB.
CC       {ECO:0000269|PubMed:20305657, ECO:0000305}.
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   -!- DISRUPTION PHENOTYPE: Cells lacking this gene display maltose
CC       accumulation. {ECO:0000269|PubMed:20305657}.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000480; ABK72477.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42768.1; -; Genomic_DNA.
DR   RefSeq; WP_011731333.1; NZ_SIJM01000033.1.
DR   RefSeq; YP_890727.1; NC_008596.1.
DR   PDB; 5JY7; X-ray; 3.60 A; I/J/K/L/M/N/O/P=1-441.
DR   PDBsum; 5JY7; -.
DR   AlphaFoldDB; A0R6D9; -.
DR   SMR; A0R6D9; -.
DR   STRING; 246196.MSMEI_6342; -.
DR   EnsemblBacteria; ABK72477; ABK72477; MSMEG_6514.
DR   EnsemblBacteria; AFP42768; AFP42768; MSMEI_6342.
DR   GeneID; 66737786; -.
DR   KEGG; msg:MSMEI_6342; -.
DR   KEGG; msm:MSMEG_6514; -.
DR   PATRIC; fig|246196.19.peg.6338; -.
DR   eggNOG; COG3281; Bacteria.
DR   OMA; TAFCDGY; -.
DR   OrthoDB; 268166at2; -.
DR   BRENDA; 2.7.1.175; 3512.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Kinase; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..441
FT                   /note="Maltokinase"
FT                   /id="PRO_0000412889"
SQ   SEQUENCE   441 AA;  48800 MW;  C2186D4AC59CE3FA CRC64;
     MSVEFEDWLT QQRWYAGRNR ELVSATTAMA VRLRDGLELV LLQANYADGP DERYQVIVAT
     GSGPIDEYSV VATIGIADGQ TAYDALYDPD ATRYLLSLID ESATVQNVRF VREPDVELPL
     DAPPRVFGAE QSNTSVVFGE DAIFKLFRRI TPGVHPDIEL NRVLARAGNP HVARLLGSFE
     TEWEGEPYAL GMVTEFAANS AEGWDMATTS TRDLFAEGDL YAEEVGGDFA GEAYRLGEAV
     ASVHACLAHE LGTEEVPFPA DVMAQRLAAA VDAVPELREH VPQIEERYHK LADTTMTVQR
     VHGDLHLGQV LRTPKGWLLI DFEGEPGQPL DERRRPDTPV RDVAGILRSF EYAAHQRLVD
     QAGDDDDRAR QLAARAREWV TRNCASFCDG YAAEAGTDPR DSADLLAAYE LDKAVYEAAY
     EARHRPSWLP IPLGSIARLL E