ID   Q46TF3_CUPPJ            Unreviewed;      1121 AA.
AC   Q46TF3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=Reut_B4228 {ECO:0000313|EMBL:AAZ63581.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ63581.1};
RN   [1] {ECO:0000313|EMBL:AAZ63581.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ63581.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) 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; CP000091; AAZ63581.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46TF3; -.
DR   STRING; 264198.Reut_B4228; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; reu:Reut_B4228; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_1_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, ECO:0000313|EMBL:AAZ63581.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          27..432
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1121 AA;  126852 MW;  6DFE8C3461E56FDB CRC64;
     MKRLTEPANA LLLNADPLWY KDAVVYQLHI KSFYDANGDG VGDFAGLLAK LDYLVDLGID
     TIWLLPFYPS PRRDDGYDIA DYRNVHPDYG TLAEARRFVG AAHARGIRVI TELVINHTSD
     QHPWFQRARK AKPGSAARRY YVWADNDQAY AGTRIIFCDT EKSNWSWDPV AGAYFWHRFY
     SHQPDLNFDN PQVMNEVLSV MRFWLDIGVD GLRLDAVPYL VEREGTTNEN LPETHTAIRH
     IRSHLDSHYQ GRVLLAEANM WPEDAQQYFG RSSTGDKGDE CHMAFHFPLM PRMYMAIARE
     DRFPITDIMR QTPELPTDCQ WAIFLRNHDE LTLEMVTSSE RDYLWEVYAS DRRARINLGI
     RRRLAPLMER DRRRIELMNS LLFSMPGTPV IYYGDEIGMG DNIHLGDRDG VRTPMQWSPD
     RNGGFSHADP ERLVLPPLQG PLYGYEAVNV EAQARDPHSL LNWMRRMLAL RRKHRAFGRG
     TLRFLFPGNR KILAYLREYE GEHILCVANL SRAPQAVELD LSAFNGRVPV EMMGATPFPA
     IGTLTYLLTL PPYGFYWFVL SEDAHPPAWH VSAPEQMPDQ ITLVLQNKGR PELTEAARRM
     LNDEVLPPYI RRRRWFGAKD DSIQRATLAY MAPFTKGTTG EEIYLGEVEV RLSGGRTERY
     QLPLGVLWDR ESADSVSQLA HGLSMARVRQ GSRVGLATDG FVLEPFAREV IRALRADAEL
     QGPQETIRFR SEPGLSAVQP EQEEIQWMSA EQSNSSLAYN NTAVLKLVRR LSGGTHPEVE
     MTRYLTAQGY PHSPPLLGEV VRTGADGVPH TLMMVQGYIL NQGNGWDWTL DYLSRVIDDA
     LPAQESADEF AEAMNGYATM AGTLGRRLAE LHAVLARPTD DPAFAPRPAT DAETRQWAEQ
     AMAAITHALA LLEKRAQNDP KSASKRFMAD VDTLLKARDA LPALVNRLAA AAPGSLQTRF
     HGDFHLGQVL IAQNDTYLVD FEGEPGQPLD WRRRKTSPLR DVAGLLRSID YAAATVGTDR
     QERTHAELPP ALAERRGGLL ERFRETASDA FLGCYRRHME ASGTPWADNA QFQPLLDLFL
     LERAAYEVEY EAANRVAWID LPASGLARMV RKLMAGNLEA Q
//