MAK_MYCVP
ID MAK_MYCVP Reviewed; 441 AA.
AC A1TH50;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Maltokinase;
DE Short=MaK;
DE EC=2.7.1.175;
DE AltName: Full=Maltose-1-phosphate synthase;
GN Name=mak; OrderedLocusNames=Mvan_5735;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
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 Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) 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; CP000511; ABM16500.1; -; Genomic_DNA.
DR RefSeq; WP_011782852.1; NC_008726.1.
DR PDB; 4U94; X-ray; 1.47 A; A=1-441.
DR PDB; 4U98; X-ray; 1.15 A; A=1-441.
DR PDB; 4WZY; X-ray; 1.71 A; A=1-441.
DR PDBsum; 4U94; -.
DR PDBsum; 4U98; -.
DR PDBsum; 4WZY; -.
DR AlphaFoldDB; A1TH50; -.
DR SMR; A1TH50; -.
DR STRING; 350058.Mvan_5735; -.
DR EnsemblBacteria; ABM16500; ABM16500; Mvan_5735.
DR KEGG; mva:Mvan_5735; -.
DR eggNOG; COG3281; Bacteria.
DR HOGENOM; CLU_029675_0_0_11; -.
DR OMA; TAFCDGY; -.
DR OrthoDB; 268166at2; -.
DR BRENDA; 2.7.1.175; 7846.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000009159; 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_0000412900"
FT HELIX 5..9
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 22..34
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 51..63
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:4U98"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 194..202
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 229..252
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:4U98"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4U98"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 340..361
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 371..395
FT /evidence="ECO:0007829|PDB:4U98"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 403..424
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:4U98"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:4U98"
SQ SEQUENCE 441 AA; 48164 MW; 9D56675BAAC943D1 CRC64;
MTLAFGDWIV HRRWYAGRSR ELVSAEPAVV TPLRDDLDHI LLDVTYTDGT VERYQLVVRW
ADSPVAGFGE AATIGTALGP QGERIAYDAL FDPDAARHLL RLVDASATVA DLRFTREPGA
TLPLYAPPKV SSAEQSNTSV IFGKDAMLKV FRRVTPGINP DIELNRVLAQ AGNRHVARLL
GSFETSWAGP GTDRCALGMV TAFAANSAEG WDMATASARE MFADVVGSDF ADESYRLGNA
VASVHATLAE ALGTSTEPFP VDTVLARLQS AARSAPELAG RAAAVEERYR RLDGRAITVQ
RVHGDLHLGQ VLRTPDDWLL IDFEGEPGQP LDERRRPDSP LRDVAGVLRS FEYAAYQKLV
ELAPEQDADG RLADRARNWV DRNSAAFCAG YAAVAGDDPR RDGDVLAAYE LDKAVYEAAY
EARFRPSWLP IPMRSIDRIL G
