ID   Q39PZ6_GEOMG            Unreviewed;      1112 AA.
AC   Q39PZ6;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 95.
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:ABB33678.1};
GN   OrderedLocusNames=Gmet_3469 {ECO:0000313|EMBL:ABB33678.1};
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB33678.1, ECO:0000313|Proteomes:UP000007073};
RN   [1] {ECO:0000313|EMBL:ABB33678.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABB33678.1, ECO:0000313|Proteomes:UP000007073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC   {ECO:0000313|Proteomes:UP000007073};
RX   PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA   Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT   "The genome sequence of Geobacter metallireducens: features of metabolism,
RT   physiology and regulation common and dissimilar to Geobacter
RT   sulfurreducens.";
RL   BMC Microbiol. 9:109-109(2009).
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; CP000148; ABB33678.1; -; Genomic_DNA.
DR   RefSeq; WP_004513920.1; NC_007517.1.
DR   AlphaFoldDB; Q39PZ6; -.
DR   STRING; 269799.Gmet_3469; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; gme:Gmet_3469; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_0_7; -.
DR   Proteomes; UP000007073; Chromosome.
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:ABB33678.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW   Transferase {ECO:0000313|EMBL:ABB33678.1}.
FT   DOMAIN          22..421
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1112 AA;  127237 MW;  7212D4627A726549 CRC64;
     MARREPLRGG NPLWYRDAII YQLHVKAFAD SDGDGMGDFR GLMGKLDYLQ SLGITAIWIL
     PFYPSPLRDD GYDIADYYSV NPSYNTLREF REFLRAAHAR RIRVITELVL NHTSDQHPWF
     QRARRAKPGS AHRDYYVWSD NPDRYQGTRI IFQDFETSNW SWDPVAKAYY WHRFYSHQPD
     LNYDNPKVQA EMLRVIDYWL GMGVDGVRLD AVPYLFEREG TNCENLPETH AFLKKLRAHV
     DASFPNRMLL GEANQWPEDA IAYFGEGDEC NMLFHFPLMP RMYMAIEMED RFPVIDIIDQ
     TPAIPEGCQW AIFLRNHDEL TLEMVTDEER DYMYRIYAAD PKARINLGIR RRLAPLMERD
     RRKIELMNAL LFSLPGTPII YYGDEIGMGD NYYLGDRNGV RTPMQWSPDR NAGFSGANPQ
     RLYLPVIIDP EYHYEAVNVE IQERNPTSLL WWMRRTIAVR RRHRAFSSGT LEMLYPANHR
     VLAFLRRHED EVILVVGNLS RFAQAVSLDL KEFAGISPAD LFSRNRFPVI REIPYPLTLG
     PHDHFWFILS RAESPRLPEG ELPRINLPGG LPWWEALQHT GGDTRLERAT TDYLNRSGWF
     RGKARAIIGY ALRDTVLLRT SDQVFPLFFL EVRYQNGAPE TYLIPVAFLR GPGAKRVDAE
     SPQAAIASLS VGDEAGILCD ALHDREFRDA LLALALGRRR LHGKRESLVV PLHGRGGHAE
     GMRETEHLIS ELVTGEEASS VILYGDRHVF KLYRTVEPGV NSEVELVRFL TEKSRYPNIV
     PFQASLELRH PGTEPCTIGL VQEYVKNQGN GWRLALHLLG QYFERILSRR GEIPPPPKRF
     SSLIDGSACT VPEPVANLIG GFYLEMAGLL GRRTAELHLA LAAGGNDPAW KPEAYSTIYQ
     RSVYQSMRNQ ARRTLQLLSQ NRNLLPIDDQ GPADRVLGAE KEILSWLAQI VGRRIGTMKI
     RIHGNFHLGK VLFTGKDFVI LDFEGEPDRT LSERRIKRSP LRDVASMIRS FHAATLTALA
     RHGNGRSGDV QLLEPWADAC YYHVSCRYLA GYLERMGNSP LVPADRNDLA TLLRSFLLDR
     ALRDLGFALG NRPETASSPL KGIETVLREY GE
//