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Database: UniProt
Entry: Q1IBT8_PSEE4
LinkDB: Q1IBT8_PSEE4
Original site: Q1IBT8_PSEE4 
ID   Q1IBT8_PSEE4            Unreviewed;      1121 AA.
AC   Q1IBT8;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   24-JAN-2024, entry version 99.
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=PSEEN2045 {ECO:0000313|EMBL:CAK14877.1};
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK14877.1, ECO:0000313|Proteomes:UP000000658};
RN   [1] {ECO:0000313|EMBL:CAK14877.1, ECO:0000313|Proteomes:UP000000658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48 {ECO:0000313|EMBL:CAK14877.1,
RC   ECO:0000313|Proteomes:UP000000658};
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(2006).
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; CT573326; CAK14877.1; -; Genomic_DNA.
DR   RefSeq; WP_011533280.1; NC_008027.1.
DR   AlphaFoldDB; Q1IBT8; -.
DR   STRING; 384676.PSEEN2045; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 32805256; -.
DR   KEGG; pen:PSEEN2045; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_1_6; -.
DR   OMA; QEDRFPI; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000658; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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   Glycosidase {ECO:0000313|EMBL:CAK14877.1};
KW   Hydrolase {ECO:0000313|EMBL:CAK14877.1};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAK14877.1};
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   1121 AA;  126378 MW;  8DD72C3105D99E7D CRC64;
     MAKRSRPAAF IDDPLWYKDA VIYQLHVKSF FDSNNDGIGD FAGLIGKLDY IAELGVNTLW
     LLPFYPSPRR DDGYDIAEYK AVHPDYGSMA DAKRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQKARHAKR GSKARDFYVW SDDDQKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPHV MKAVIDVMRF WLDIGVDGLR LDAIPYLIER DGTNNENLPE THVVLKAIRA
     EIDANYPDRM LLAEANQWPE DTRPYFGEGD GDECHMAFHF PLMPRMYMAL AMEDRFPITD
     ILRQTPEIPA NCQWAIFLRN HDELTLEMVT DRERDYLWNY YAEDRRARIN LGIRRRLAPL
     LQRDRRRIEL LTSLLLSMPG TPTLYYGDEL GMGDNIYLGD RDGVRTPMQW SPDRNGGFSR
     ADPQRLVLPP IMDPLYGYQT INVEAQAHDP HSLLNWNRRL LAVRSQQQAF GRGSMKMLSP
     SNRRILAYLR EYTDANGNNE IVLCVANVSR TAQAAELELS QYADKVPVEM LGGSAFPPIG
     QLPFLLTLPP YGFYWFLLAP HDRMPSWHIQ PSEGLPELTT LVLRKRLEEL LETPSRDTLE
     QAILPQYLPK RRWFAGKEGP LDQVRLHYGV RFATATLPTL LAELEVHSEG VVSHYQLPFG
     LLPEEQISAA PPQQLALSRV RRGRQVGLIT DAFVLEPFVR AVLQACQGNT RLPCGDGLGE
     LHFTCTPQLA ALGIDDESEV RYLSAEQSNS SVVVGGSLVL KLIRRVNPGI HPELEMSAYL
     TAAGFANISP LLAWVSRVDA AGEPHLLMIA QGYLSNQGDA WGWTQNTLER AIRDQMEPAT
     GEADAHTDAL VELTGFAALL GQRLGEMHLL LAAPTEDPAF QPRASDEQDS QRWNRQINAE
     LNHALDLLAE HRAALDGDSQ ALVDELLQQR EGLAQHIGNL ARQAQGGVLM RVHGDLHLGQ
     VLVVQGDAYL IDFEGEPSRP LDQRRARHSP YKDVSGVLRS FDYAAAMILR SASAVDLSDA
     ARQARQRVAR QYLHQSRHAF VEAYGLATAA MPHAWQQADG ARAALELFCL EKAAYEITYE
     AENRPGWLAV PLHGLHGLSR SGFSRDEGSA VPGTRSAGDR G
//
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