MAK_MYCBO
ID MAK_MYCBO Reviewed; 455 AA.
AC Q7U2S7; A0A1R3XUE1; X2BE38;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Maltokinase;
DE Short=MaK;
DE EC=2.7.1.175;
DE AltName: Full=Maltose-1-phosphate synthase;
GN Name=mak; OrderedLocusNames=BQ2027_MB0132;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION AS A MALTOKINASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND GENE NAME.
RC STRAIN=BCG / ATCC 27289 / DSM 43990;
RX PubMed=20507595; DOI=10.1186/1471-2091-11-21;
RA Mendes V., Maranha A., Lamosa P., da Costa M.S., Empadinhas N.;
RT "Biochemical characterization of the maltokinase from Mycobacterium bovis
RT BCG.";
RL BMC Biochem. 11:21-21(2010).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of maltose to
CC maltose 1-phosphate. It uses ATP, GTP and UTP as phosphate donors with
CC comparable but decreasing efficiency. Is probably involved in a
CC branched alpha-glucan biosynthetic pathway from trehalose, together
CC with TreS, GlgE and GlgB. {ECO:0000269|PubMed:20507595}.
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:20507595};
CC -!- ACTIVITY REGULATION: Inhibited by glycerol and zinc ions.
CC {ECO:0000269|PubMed:20507595}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.74 mM for ATP (at 37 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:20507595};
CC KM=1.01 mM for GTP (at 37 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:20507595};
CC KM=1.30 mM for UTP (at 37 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:20507595};
CC KM=2.52 mM for maltose (at 37 degrees Celsius and at pH 8)
CC {ECO:0000269|PubMed:20507595};
CC Vmax=21.42 umol/min/mg enzyme with ATP as substrate (at 37 degrees
CC Celsius and at pH 8) {ECO:0000269|PubMed:20507595};
CC Vmax=21.05 umol/min/mg enzyme with maltose as substrate (at 37
CC degrees Celsius and at pH 8) {ECO:0000269|PubMed:20507595};
CC Vmax=18.65 umol/min/mg enzyme with GTP as substrate (at 37 degrees
CC Celsius and at pH 8) {ECO:0000269|PubMed:20507595};
CC Vmax=7.07 umol/min/mg enzyme with UTP as substrate (at 37 degrees
CC Celsius and at pH 8) {ECO:0000269|PubMed:20507595};
CC pH dependence:
CC Optimum pH is between 7 and 9. The enzyme is active between pH 6 and
CC 11. {ECO:0000269|PubMed:20507595};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius. The enzyme is active
CC between 20 and 65 degrees Celsius. {ECO:0000269|PubMed:20507595};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20507595}.
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIT98554.1; -; Genomic_DNA.
DR RefSeq; NP_853799.1; NC_002945.3.
DR RefSeq; WP_003899824.1; NC_002945.4.
DR AlphaFoldDB; Q7U2S7; -.
DR SMR; Q7U2S7; -.
DR PATRIC; fig|233413.5.peg.148; -.
DR OMA; TAFCDGY; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001419; 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; 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; Glycogen biosynthesis;
KW Glycogen metabolism; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..455
FT /note="Maltokinase"
FT /id="PRO_0000412883"
SQ SEQUENCE 455 AA; 49889 MW; FE561A06279FC6B9 CRC64;
MTRSDTLATK LPWSDWLPRQ RWYAGRNREL ATVKPGVVVA LRHNLDLVLV DVTYTDGATE
RYQVLVGWDF EPASEYGTKA AIGVADDRTG FDALYDVAGP QFLLSLIVSS AVCGTSTGEV
TFTREPDVEL PFAAQPRVCD AEQSNTSVIF DRRAILKVFR RVSSGINPDI ELNRVLTRAG
NPHVARLLGA YQFGRPNRSP TDALAYALGM VTEYEANAAE GWAMATASVR DLFAEGDLYA
HEVGGDFAGE SYRLGEAVAS VHATLADSLG TAQATFPVDR MLARLSSTVA VVPELREYAP
TIEQQFQKLA AEAITVQRVH GDLHLGQVLR TPESWLLIDF EGEPGQPLDE RRAPDSPLRD
VAGVLRSFEY AAYGPLVDQA TDKQLAARAR EWVERNRAAF CDGYAVASGI DPRDSALLLG
AYELDKAVYE TGYETRHRPG WLPIPLRSIA RLTAS
