ID   Q3KD79_PSEPF            Unreviewed;      1113 AA.
AC   Q3KD79;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-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=Pfl01_2535 {ECO:0000313|EMBL:ABA74276.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA74276.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA74276.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA74276.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA74276.1; -; Genomic_DNA.
DR   RefSeq; WP_011333954.1; NC_007492.2.
DR   AlphaFoldDB; Q3KD79; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; pfo:Pfl01_2535; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_2_6; -.
DR   Proteomes; UP000002704; Chromosome.
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:ABA74276.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          24..425
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1113 AA;  125038 MW;  E31F28BA43067E8B CRC64;
     MAKKPKAATF IKDPLWYKDA VIYQVHVKSF FDSNNDGIGD FPGLIAKLDY IADLGVNTIW
     LLPFYPSPRR DDGYDIAEYR GVHSDYGTMA DAKRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQRARKAKP GSAARDFYVW SDDDQKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPQV MKAVLSVMRY WLDMGIDGLR LDAIPYLIER DGTNNENLPE THDVLKQIRA
     EIDANYPDRM LLAEANQWPE DTQLYFGDTD AEGVNGDECH MAFHFPLMPR MYMALAQEDR
     FPITDILRQT PEIPANCQWA IFLRNHDELT LEMVTDKERD YLWNYYAADR RARINLGIRR
     RLAPLMERDR RRIELLNSLL LSMPGTPTLY YGDEIGMGDN IYLGDRDGVR TPMQWSIDRN
     GGFSRADPAS LVLPPIMDPQ YGYQSVNVET QAGDPHSLLN WTRRLLAVRK QSKAFGRGTL
     KMLSPANRRV LAYTREYTGP DGKHEIILCV ANVSRSAQAV ELDLSAYVGM VPVEMLGGNA
     FPPIGQLSFL LTLPPYGFYW FGLAAENQMP SWHVEPAQSL PDFTTLVLKK RMEELLEAPS
     RATLEQAILP SWLQNRRWFA GKDADIEQVK LAYGVRFGDA QHPVLFSEIE VQSGGQTSRY
     QLPFGFISED QVGPALPQQL ALARVRRVRQ VGLITDAFSL EAFIRAVLQG MQGGTVLESI
     EGEIRFEATP QLEKLGLGAE SEVRYLSAEQ SNSSVVIGNS LVLKLIRKVA SGVHPELEMS
     AYLTAAGFAN ISPLLGSVIR RDGKGEDNLL MIAQGYLSNQ GDAWEWTQNN LERALRDELA
     DAVSEQAQHY NALGELKDFA GMLGQRLGEM HQVLAAPSDN QDFAPQVSSA KDAQATGKDV
     AAQVEHALKL LKQHQGELDA ADQKLVGRLL DHKKAILAHV QELAKQSAGG LRIRVHGDLH
     LGQVLVIKGD AYLIDFEGEP ARPLAERRGK HSPYKDVSGV LRSFDYAAAM ALNVHNVDNS
     PEAEAARRRV TERYLREARE AFLQAYRQAA ASLDHAWQDP EGADAALALF GLEKAAYEVA
     YEAENRPTWL PVPLHGLYGL LTGLKPFSDL GGE
//