ID   F2K9Q8_PSEBN            Unreviewed;      1114 AA.
AC   F2K9Q8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   ORFNames=PSEBR_a1899 {ECO:0000313|EMBL:AEA68120.1};
OS   Pseudomonas brassicacearum (strain NFM421).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=994484 {ECO:0000313|EMBL:AEA68120.1, ECO:0000313|Proteomes:UP000006692};
RN   [1] {ECO:0000313|EMBL:AEA68120.1, ECO:0000313|Proteomes:UP000006692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NFM421 {ECO:0000313|EMBL:AEA68120.1,
RC   ECO:0000313|Proteomes:UP000006692};
RX   PubMed=21515771; DOI=10.1128/JB.00411-11;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Vacherie B.,
RA   Santaella C., Heulin T., Achouak W.;
RT   "Complete genome sequence of a beneficial plant root-associated bacterium,
RT   Pseudomonas brassicacearum.";
RL   J. Bacteriol. 193:3146-3146(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NFM421;
RA   Ortet P., Barakat M., Lalaouna D., Fochesato S., Barbe V., Santaella C.,
RA   Heulin T., Achouak W.;
RT   "Complete Genome Sequence of a beneficial plant roots-associated bacterium
RT   Pseudomonas brassicacearum.";
RL   Submitted (MAR-2011) 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; CP002585; AEA68120.1; -; Genomic_DNA.
DR   RefSeq; WP_003200104.1; NC_015379.1.
DR   AlphaFoldDB; F2K9Q8; -.
DR   STRING; 994484.PSEBR_a1899; -.
DR   GeneID; 57258646; -.
DR   KEGG; pba:PSEBR_a1899; -.
DR   HOGENOM; CLU_007635_2_2_6; -.
DR   Proteomes; UP000006692; 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:0016740; F:transferase activity; 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};
KW   Transferase {ECO:0000313|EMBL:AEA68120.1}.
FT   DOMAIN          24..425
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1114 AA;  125264 MW;  D475E4E0B3A484FD CRC64;
     MAKKPRSATF IKDPLWYKDA VIYQVHVKSY FDSNNDGIGD FPGLIEKLDY IADLGVNTIW
     LLPFYPSPRR DDGYDIAEYR GVSPDYGTMA DARRFIAEAH KRNLRVITEL VINHTSDQHP
     WFQRARKAKP GSKARDFYVW SDDDHKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPQV LKAVLSVMRY WLDMGIDGLR LDAIPYLIER DGTNNENLPE THDVLKLIRA
     EIDANYPDRM LLAEANQWPE DTQLYFGDVD AQGMNGDECH MAFHFPLMPR MYMALAQEDR
     FPITDILRQT PEIPANCQWA IFLRNHDELT LEMVTDKERD YLWNYYAADR RARINLGIRR
     RLAPLVERDR RRVELLNSLL LSMPGTPTLY YGDEIGMGDN IYLGDRDGVR TPMQWSIDRN
     GGFSRADPAS LVLPPIMDPQ YGYQSVNVET QAGDPHSLLN WTRRMLAVRK QSKAFGRGTL
     KMLSPSNRRI LAYTREYTGP DGKHEIILCV ANVSRSAQAA ELDLSTYAGM VPVEMLGGNA
     FPPIGQLNFL LTLAPYGFYW FALATENQMP SWHVEPAQSL PDFTTLVLKK RLEELLEAPS
     RTTLEQTILP SWLQNRRWFA GKDSAIEKVE IVYGVRFGDP QHPVLLSEID VTSGGQTLRY
     QLPFGLLAED QVGAALPQQL ALSRVRRVRQ VGLITDAFSL ESFVRAVLHS MQAATVLPFA
     EGELRFEPTE GLAALNLGEE PEVRYLSAEQ SNSSVVVGSS LVLKLIRKVA SGVHPELEMS
     AYLTAAGFSN ISPLLGSVVR RDVQGEDALL MIAQGYLSNQ GDAWEWTQNN LERALRDELA
     DAVSEQEQHY NALGELKDFA GMLGQRLGEM HQVLAQATDD PDFAPQATNA KQAQAIGKDV
     AAQVENALRL LKQNQGQLNP ADQAMVARLL EHKKTVLAHV QTLAGKAEGG LRIRVHGDLH
     LGQVLVIKGD AYLIDFEGEP ARPLHERRGK HSPYKDVSGV LRSFDYAAAM AIHLHTVDST
     ADADAARQRV ADRYLKEARQ AFVEAYRLAA ASLAHEWKDA EGEDAALALF GLEKAAYEVA
     YEAENRPTWL PVPLHGLVGL LSGLQPFSDV AGPI
//