ID   B1J6R5_PSEPW            Unreviewed;      1105 AA.
AC   B1J6R5;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=PputW619_1816 {ECO:0000313|EMBL:ACA72320.1};
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235 {ECO:0000313|EMBL:ACA72320.1};
RN   [1] {ECO:0000313|EMBL:ACA72320.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W619 {ECO:0000313|EMBL:ACA72320.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Psuedomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA72320.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1J6R5; -.
DR   STRING; 390235.PputW619_1816; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ppw:PputW619_1816; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_1_6; -.
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};
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   1105 AA;  124932 MW;  607DB1CE0FD46BBC CRC64;
     MAKRSRPAAF LDDPLWYKDA VIYQLHIKSF FDANNDGIGD FAGLISKLDY IADLGVNTLW
     LLPFYPSPRR DDGYDIAEYK AVHPDYGSMA DARRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQRARHAKR GSKARDFYVW SDDDQKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPQV LKAVIGVMRF WLDLGVDGLR LDAIPYLIER DGTNNENLPE THKVLKAIRA
     EIDANYPDRM LLAEANQWPE DTRPYFGEGD GDECHMAFHF PLMPRMYMAL AMEDRFPITD
     ILRQTPEIPA NCQWAIFLRN HDELTLEMVT DRERDYLWNY YAQDRRARIN LGIRRRLAPL
     LQRDRRRIEL LTSLLLSMPG TPTLYYGDEL GMGDNIYLGD RDGVRTPMQW SPDRNGGFSK
     ADPQRLVLPP IMDPLYGYQT VNVEAQAHDP HSLLNWNRRL LAVRNQQKAF GRGTLRTLAP
     SNRRILAYIR EYTDAEGNSE VILCVANVSR AAQAAELELS QYADKVPVEM LGGSAFPPIG
     QLPFLLTLPP YAFYWFLLAA HDRMPSWHVQ ATEGLPELTT LVLRKRMEEL LETPSSDTLQ
     DAILPQYLPK RRWFAGKEGP VDQVRLCYGV RLGTATTPVL LSEIEVLGDG VANRYQLPFG
     LLPEDQINSA LPQQLAMSRV RRGRQVGLIT DAFVLEPFIR AVLRACQDGL RLPCGNGQGE
     LRFHCTEALA SLGLDEDSAV RYLSAEQSNS SVVVGDRVVL KLIRRVNPGV HPELEMSAYL
     TAAGFANISP LLAWVSRVDE TDAPHLLMIA QGYLSNQGDA WAWTQNTLER AIRDEMEPSS
     NDGEAHTDAL AELNGFAALL GQRLGEMHLL LAAPTDDPAF RPRSSDGEDS ERWAQQISSE
     LCHALDLLAQ HRDSLDNDSQ ALVDDLQQQR EGLAQHIANL ARQAQGGLLM RVHGDLHLGQ
     VLVVQGDAYL IDFEGEPSRA LQERRAKHSP YKDVSGVLRS FDYAAAMILR SASAVDASEA
     ARQARQRVAR QYLHQSRHAF VEAYGLATAA MPHAWQQAEG ERAALELFCL EKAAYEITYE
     AENRPSWLAV PLHGLHGLIS TWGES
//