ID   A2S3L3_BURM9            Unreviewed;      1131 AA.
AC   A2S3L3;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Maltokinase {ECO:0000256|ARBA:ARBA00013882};
DE            EC=2.7.1.175 {ECO:0000256|ARBA:ARBA00011962};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
DE   AltName: Full=Maltose-1-phosphate synthase {ECO:0000256|ARBA:ARBA00031251};
GN   Name=treS {ECO:0000313|EMBL:ABN02577.1};
GN   OrderedLocusNames=BMA10229_A0534 {ECO:0000313|EMBL:ABN02577.1};
OS   Burkholderia mallei (strain NCTC 10229).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=412022 {ECO:0000313|EMBL:ABN02577.1, ECO:0000313|Proteomes:UP000002283};
RN   [1] {ECO:0000313|EMBL:ABN02577.1, ECO:0000313|Proteomes:UP000002283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 10229 {ECO:0000313|EMBL:ABN02577.1,
RC   ECO:0000313|Proteomes:UP000002283};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001537};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; CP000546; ABN02577.1; -; Genomic_DNA.
DR   RefSeq; WP_004205216.1; NC_008836.1.
DR   AlphaFoldDB; A2S3L3; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 56595323; -.
DR   KEGG; bml:BMA10229_A0534; -.
DR   HOGENOM; CLU_007635_0_0_4; -.
DR   Proteomes; UP000002283; Chromosome I.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR040999; Mak_N_cap.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   InterPro; IPR012811; TreS_maltokin_C_dom.
DR   NCBIfam; TIGR02457; TreS_Cterm; 1.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF18085; Mak_N_cap; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Kinase {ECO:0000313|EMBL:ABN02577.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Transferase {ECO:0000313|EMBL:ABN02577.1}.
FT   DOMAIN          48..442
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1131 AA;  126731 MW;  99250179A9716A92 CRC64;
     MKPADTLEDV GRAQFVAHMA RRPRRARRRE APGVADTPLW YKDAIIYQLH VKSFFDANND
     GVGDFAGLIA KLDYIAELGV DTVWLLPFYP SPRRDDGYDI ADYRGVHPDY GTLADVRRFI
     REAHARGLRV ITELVINHTS DQHPWFQRAR RAKRGSVHRD YYVWSDTDLK YAGTRIIFLD
     TETSNWTHDP VAGQYYWHRF YSHQPDLNFD NPAVVREVLQ IMRFWLDLGI DGLRLDAVPY
     LVEREGTSNE NLPQTHAILK LIRATIDAEY PNRMLLAEAN QWPEDVQEYF GDEDECHMAF
     HFPLMPRIYM SIASEDRFPI IDIMRQTPAL APSNQWAVFL RNHDELTLEM VTDSERDLLW
     QAYASERRAR LNLGIRRRLA PLMERDRRRI ELINSILLSM PGTPVIYYGD ELGMGDNLHL
     GDRDGVRTPM QWSSDRNGGF SRADPELLVL PPVMGTLYGY DAINVEAQTR DPHSLLNWTR
     RILSTRRATR VFGRGAIRFL RPGNRKILAY LRELDGETPV LCVANLSRAS QAVELDLSEF
     AGCVPTEMTS DSPFPPIGQL PYLLTFPPYG FLWFALSEHG REPAWHQQYA EPLPEYLTLV
     MRRGETQPGA ALLDTLAQDA LPSWLARRRW FASKERRVDS ARFDALTPIP GEPFQYAEAR
     VAVDGREERY VVPLASAWGS ETPQPLFAQL ALARVRRGHT VGLLTDAFAL PSFAHGVLRQ
     LRAGAAVPVA GGGRLEFRPE PDLARLDPGD APGVRWFAAE QSNSSLVIGE AIVLKIVRKL
     ATGVHPEAEM GRHLRRIGYR NVAPLVGEVV RIGADGAPHT VAILQEYVDN QGDAWTRSCD
     FLKRAIEELA LPAANDADAA APSAEPEMID GYATFAGIVG KRLGELHAAL AQPSDDAAFA
     PQRVSPARVD GWIGDALGWF ERAASLLAER LDTLEGQTRA AAELLVAQRA AVAEALRALV
     PRELDGCCIR IHGDFHLGQV LDVQGDALLI DFEGEPARPL GQRRAQSHPL RDVAGFLRSL
     SYASAAAQFT IEKAPQQAAE RKRALFERFG QAAADRFVAQ YREALSAASR EFVEPRYADR
     LLALFLIEKA SYELCYEAAN RPDWLSVPAN GLAALVARLI GGAAPQQEDA R
//