ID   E1TGE5_BURSG            Unreviewed;      1156 AA.
AC   E1TGE5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
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   OrderedLocusNames=BC1003_4572 {ECO:0000313|EMBL:ADN60504.1};
OS   Burkholderia sp. (strain CCGE1003).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN60504.1};
RN   [1] {ECO:0000313|EMBL:ADN60504.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN60504.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL   Submitted (SEP-2010) 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; CP002218; ADN60504.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1TGE5; -.
DR   STRING; 640512.BC1003_4572; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; bgf:BC1003_4572; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_0_0_4; -.
DR   OrthoDB; 9805159at2; -.
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   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          50..463
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  129827 MW;  848140B0E20F3CFB CRC64;
     MKRDDPSQTT TQAPVGNAPG NTAKPRTKRR GKPTALADDP LWYKDAIIYQ VHIKSFFDAN
     NDGVGDFPGL IAKLDYIAEL GVNAIWLLPF YPSPRRDDGY DIADYRNVHP DYGQLSDVKR
     FIQEAHARGI RVITELVINH TSDQHPWFQR ARRAKPGSNH RNFYVWSDTD QKYPETRIIF
     IDSEPSNWTH DPVAGAYYWH RFYSHQPDLN FDNPAVLREV LQIMRFWLDM GIDGLRLDAV
     PYLVEREGTN NENLPETHAI LKKIRATIDA EYPNRMLLAE ANQWPEDVKE YFGDEDECHM
     AFHFPLMPRI YMSIASEDRF PITDIMRQTP DLAASNQWAI FLRNHDELTL EMVTDSERDY
     LWNTYASDRR ARLNLGIRRR LAPLMERDRR RIELINSLLL SMPGTPVIYY GDELGMGDNI
     HLGDRDGVRT PMQWSSDRNG GFSRADPEQL VLPPVMGSLY GFDAVNVEAQ SRDPHSLLNW
     TRRMLATRRA KQTFGRGTIR FLKPENRKIL AYLREMPGEP PILCVANLSR APQAVELDLS
     EFNGAVPIEM TADSVFPAIG QLTYLLTFPP YGFLWFLLCE GGQRPTWAQA HPEPLPEFVT
     IVIREGQAGP TPENVRLLES EVLPSWLSRR RWFASKDQKM HAVRLAALTT IPNGGFAFTE
     IEADVGDHTE RYVVPIAITW GGETTTPLFL QLALARVRRG RNVGHLTDAF ALPIFAHGVL
     RKLRERAVVP TVQKSEIRFI PTDRFAELDN LGERPEVRWL AAEQSNSSLI VADAAVLKLV
     RRLVSGIHPE AEISRYLTQL GYANTAPLFG EVVRVDPEGV PHTLAILQGF VDNQGDAWNW
     SLDYLRRSVD ELAITVDTEA TAPPDRDNEA ILLEGYSALA GIIGRRLGEL HVALSSPTDD
     PAFSPEPASA EQVKAWVDGT QSMLASALDL LAPRVEQLLD ADTKALAQSL IDRRAALVEA
     VNKLVAPDVQ ALRIRIHGDF HLGQVLVAQG DAYLIDFEGE PARSLEERRQ KSSPLRDVAG
     LMRSLSYASA AAQSTTEAAP QQTADRKRVL FDRFRAHATD TFLREYRAAT AEAPTPLVAP
     EAEQALLDLF LIEKAAYEVR YEAANRPTWL SLPVRGLAAL ASRLLGDTGA PHAAHDSSTQ
     APDAATPPHP AEGDYE
//