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
//
