ID   D5WEP3_PARAM            Unreviewed;      1155 AA.
AC   D5WEP3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=BC1002_5229 {ECO:0000313|EMBL:ADG19168.1};
OS   Paraburkholderia atlantica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2654982 {ECO:0000313|EMBL:ADG19168.1, ECO:0000313|Proteomes:UP000002190};
RN   [1] {ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|Proteomes:UP000002190};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Martinez-Romero E., Hernandez M.A.R.,
RA   Tiedje J.M., Woyke T.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. CCGE1002.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG19168.1, ECO:0000313|Proteomes:UP000002190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCGE1002 {ECO:0000313|EMBL:ADG19168.1,
RC   ECO:0000313|Proteomes:UP000002190};
RX   PubMed=23209196; DOI=10.1128/JB.01756-12;
RA   Ormeno-Orrillo E., Rogel M.A., Chueire L.M., Tiedje J.M.,
RA   Martinez-Romero E., Hungria M.;
RT   "Genome Sequences of Burkholderia sp. Strains CCGE1002 and H160, Isolated
RT   from Legume Nodules in Mexico and Brazil.";
RL   J. Bacteriol. 194:6927-6927(2012).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002014; ADG19168.1; -; Genomic_DNA.
DR   RefSeq; WP_013092960.1; NC_014118.1.
DR   AlphaFoldDB; D5WEP3; -.
DR   STRING; 640511.BC1002_5229; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; bge:BC1002_5229; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_0_0_4; -.
DR   Proteomes; UP000002190; Chromosome 2.
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..444
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1128..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1155 AA;  129991 MW;  B916F56743C72D52 CRC64;
     MKRDDPAQST HEAQTAAAVG TAAKVRTRRR GKPAALSDDP LWYKDAIIYQ VHIKSFFDAN
     NDGVGDFPGL IAKLDYIAEL GVNAIWLLPF YPSPRRDDGY DIADYRNVHP DYGQLADVRR
     FIQEAHARGI RVITELVINH TSDQHPWFQR ARRAKAGSNY RNYYVWSDTD QKYAETRIIF
     IDSEPSNWTH DPVAGAYYWH RFYSHQPDLN FDNPAVMREV LQVMRFWLDM GIDGLRLDAV
     PYLVEREGTN NENLPETHEI LKRIRATIDA EYPNRMLLAE ANQWPEDVKE YFGNEDECHM
     AFHFPLMPRI YMSIASEDRF PITDIMKQTP DLPNSNQWAI FLRNHDELTL EMVTDSERDY
     LWNTYASDRR ARLNLGIRRR LAPLMERDRR RIELINSLLL SMPGTPVIYY GDELGMGDNI
     HLGDRDGVRT PMQWSSDRNG GFSRADPELL VLPPVMGTLY GFDAVNVEAQ SRDPHSLLNW
     TRRMLSTRRS KQTFGRGTIR FLKPENRKIL AYLREMPGEA PILCVANLSR APQAVELDLS
     EFNGFVPIEM TADSVFPAIG QLTYLLTFPP YGFLWFMLCE GGGRPTWAQA HSEPLPEFVT
     IVIREGQTGP TPENVRLLES EVLPSWLSRR RWFASKDQKM HAVRLAALTT IPNGGFAFTE
     IEADVGDHTE RYVVPIALTW GGETTTPLFL QLALARVRRG RTVGHLTDAF SLPIFAHNVL
     RKMREHAVVP TVQKSEIKFL PTERFTELDN LGERPEIRWL AAEQSNSSLI IADAAVLKLV
     RRLVSGIHPE AEISRYLTQL GYANTAPLYG EVVRVDPEGV PHTLAILQGF IDNQGDAWNW
     SLDYLRRSVD ELAIAVDTET QTAPDRTNES ILLDGYGELA GIIGRRLGEL HVALATPSDD
     PAFAPEHANA EQVKTWVDAT QTMLASALDL LAPRIADMSD PDTKGLAQSL IDRRAALVEA
     VDNLVPGDAG ALRIRIHGDF HLGQVLVAHG DAYLIDFEGE PARSLEERRQ KSSPLRDVAG
     LMRSLSYASA AAQSTTESAP QQTADRKRAL FERFRSHATT AFLAEYRAAA AQSSEPLVAP
     ESEEALLDLF LIEKAAYEIR YEAANRPTWL GLPVRGLAAL TSRLLGDTGA PPHYDPSTRV
     SGSATPPNPA EGDYE
//