MAK1_MYCTU
ID MAK1_MYCTU Reviewed; 455 AA.
AC O07177; L0T5L4;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Maltokinase;
DE Short=MaK;
DE EC=2.7.1.175;
DE AltName: Full=Maltose-1-phosphate synthase;
GN Name=mak; OrderedLocusNames=Rv0127;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP GENE NAME.
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).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of maltose to
CC maltose 1-phosphate (By similarity). Is involved in a branched alpha-
CC glucan biosynthetic pathway from trehalose, together with TreS, GlgE
CC and GlgB. {ECO:0000250, ECO:0000269|PubMed:20305657}.
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 -!- INTERACTION:
CC O07177; Q80XK6: Atg2b; Xeno; NbExp=3; IntAct=EBI-25767633, EBI-11566520;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP42852.1; -; Genomic_DNA.
DR PIR; H70983; H70983.
DR RefSeq; NP_214641.1; NC_000962.3.
DR RefSeq; WP_003916610.1; NZ_NVQJ01000001.1.
DR PDB; 4O7O; X-ray; 2.40 A; A/B=1-455.
DR PDB; 4O7P; X-ray; 2.90 A; A/B=1-455.
DR PDBsum; 4O7O; -.
DR PDBsum; 4O7P; -.
DR AlphaFoldDB; O07177; -.
DR SMR; O07177; -.
DR IntAct; O07177; 12.
DR MINT; O07177; -.
DR STRING; 83332.Rv0127; -.
DR PaxDb; O07177; -.
DR DNASU; 886880; -.
DR GeneID; 886880; -.
DR KEGG; mtu:Rv0127; -.
DR TubercuList; Rv0127; -.
DR eggNOG; COG3281; Bacteria.
DR InParanoid; O07177; -.
DR OMA; TAFCDGY; -.
DR PhylomeDB; O07177; -.
DR BioCyc; MetaCyc:G185E-4244-MON; -.
DR BRENDA; 2.7.1.175; 3445.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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 3D-structure; ATP-binding; Carbohydrate metabolism; Glycogen biosynthesis;
KW Glycogen metabolism; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..455
FT /note="Maltokinase"
FT /id="PRO_0000412894"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:4O7P"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 59..69
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 138..141
FT /evidence="ECO:0007829|PDB:4O7O"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 145..162
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 168..178
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 204..215
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:4O7O"
FT TURN 237..242
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 248..269
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 278..291
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:4O7O"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 357..373
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:4O7O"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 383..408
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 416..437
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:4O7O"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:4O7O"
SQ SEQUENCE 455 AA; 49879 MW; 7D643689E94F5ED4 CRC64;
MTRSDTLATK LPWSDWLSRQ 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
