ID   F8G643_PSEP6            Unreviewed;      1105 AA.
AC   F8G643;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=PPS_3464 {ECO:0000313|EMBL:AEJ14011.1};
OS   Pseudomonas putida (strain DSM 28022 / S16).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042876 {ECO:0000313|EMBL:AEJ14011.1, ECO:0000313|Proteomes:UP000000502};
RN   [1] {ECO:0000313|EMBL:AEJ14011.1, ECO:0000313|Proteomes:UP000000502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S16 {ECO:0000313|EMBL:AEJ14011.1,
RC   ECO:0000313|Proteomes:UP000000502};
RX   PubMed=21914868; DOI=10.1128/JB.05663-11;
RA   Yu H., Tang H., Wang L., Yao Y., Wu G., Xu P.;
RT   "Complete genome sequence of the nicotine-degrading Pseudomonas putida
RT   strain S16.";
RL   J. Bacteriol. 193:5541-5542(2011).
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; CP002870; AEJ14011.1; -; Genomic_DNA.
DR   RefSeq; WP_013973335.1; NC_015733.1.
DR   AlphaFoldDB; F8G643; -.
DR   KEGG; ppt:PPS_3464; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_1_6; -.
DR   Proteomes; UP000000502; 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};
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;  124962 MW;  AD396EB8AD66D43B CRC64;
     MAKRSRPAAF IDDPLWYKDA VIYQLHIKSF FDSNNDGIGD FAGLISKLDY IAELGVNTLW
     LLPFYPSPRR DDGYDIAEYK AVHPDYGNLA DARRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQRARHAKR GSKARDFYVW SDDDQKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPQV LKAVIGVMRF WLDLGVDGLR LDAIPYLIER DGTNNENLAE THDVLKAIRA
     EIDANYPDRM LLAEANQWPE DTRPYFGEGE GDECHMAFHF PLMPRMYMAL AMEDRFPITD
     ILRQTPEIPA NCQWAIFLRN HDELTLEMVT DRERDYLWNY YAEDRRARIN LGIRRRLAPL
     LQRDRRRIEL LTSLLLSMPG TPTLYYGDEL GMGDNIYLGD RDGVRTPMQW SPDRNGGFSR
     ADPQRLVLPP IMDPLYGYQT VNVEAQANDP HSLLNWTRRM LAVRKQQKAF GRGSLRTLTP
     NNRRILAYLR EYTDADGNTE VILCVANVSR AAQAAELELS QYADKVPVEM LGGSAFPPIG
     QLPFLLTLPP YAFYWFLLAS HDRMPSWHIQ ATEGLPELTT LVLRKRMEEL LEAPSSDTLQ
     SAILPQYLPK RRWFAGKEGP IDQVRLCYGV RFGTATTPVL LGEIEVLSEG VATRYQLPFG
     LLPEEQISTA LPQQLALARV RRAHQVGLIT DAFVLEPFIR AVLRACEGGM HLPCGNGEGE
     LRFESTQQLA SLALNDESSV RYLSAEQSNS SVVIGDQVVL KLIRRVNPGV HPELEMSAYL
     TAAGFANISP LLAWVSRVDE QGAPHLLMIA QGYLSNQGDA WAWTQNTLER AIRDQMEPSS
     LDADAHTDAL AELTGFAALL GQRLGEMHLL LAAPTNDEAF QPRPSDADDS ERWSAQISAE
     LTHALDLLAQ HRDSLDSESQ ALVDDLQQQR DGLAQHIANL TRQAQGGLLM RVHGDLHLGQ
     VLVVQGDAYL IDFEGEPARP LQERRAKHSP YKDVSGVLRS FDYAAAMILR SASAVDLSDP
     ARQARQRVAR QYLHQSRHAF VEAYGLATAA MPHAWQQAEG ERAALELFCL EKAAYEITYE
     AENRPSWLAV PLHGLHGLIS TWGES
//