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Entry: A0A077FDG5_9PSED
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ID   A0A077FDG5_9PSED        Unreviewed;      1103 AA.
AC   A0A077FDG5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
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=PSAKL28_21000 {ECO:0000313|EMBL:AIL61321.1};
OS   Pseudomonas alkylphenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL61321.1, ECO:0000313|Proteomes:UP000028931};
RN   [1] {ECO:0000313|EMBL:AIL61321.1, ECO:0000313|Proteomes:UP000028931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KL28 {ECO:0000313|EMBL:AIL61321.1,
RC   ECO:0000313|Proteomes:UP000028931};
RA   Lee K., Lim J.Y., Hwang I.;
RL   Submitted (JUL-2014) 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; CP009048; AIL61321.1; -; Genomic_DNA.
DR   RefSeq; WP_038609940.1; NZ_CP009048.1.
DR   AlphaFoldDB; A0A077FDG5; -.
DR   KEGG; palk:PSAKL28_21000; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_2_1_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000028931; 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   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   1103 AA;  124618 MW;  D7F37657529CD642 CRC64;
     MAKRNRPAAF IDDPLWYKDA IIYQVHVKSF FDSNNDGIGD FPGLIAKLDY IAELGVNTLW
     LLPFYPSPRR DDGYDIAEYK AVHPDYGTLA DVKRFIAEAH KRGLRVITEL VINHTSDQHP
     WFQRARRAKP GSKARDFYVW SDTDQKYDGT RIIFLDTEKS NWTWDPVAGQ YFWHRFYSHQ
     PDLNFDNPQV LKAVIEVMRY WLDLGIDGLR LDAIPYLIER DGTNNENLPE THQVLKQIRA
     EIDANYPDRM LLAEANQWPE DTQLYFGEGQ GDECHMAFHF PLMPRMYMAV AQEDRFPITD
     ILRQTPEIPA NCQWAIFLRN HDELTLEMVT DRERDYLWNY YAEDRRARIN LGIRRRLAPL
     LQRDRRRVEL LSSLLLSMPG TPTLYYGDEI GMGDNIYLGD RDGVRTPMQW SIDRNGGFSR
     ADPARLVLPP IMDPLYGFAS VNVEAQAHDP HSLLNWNRRL LAVRKQQKAF GRGSLRMLSP
     SNRRILAYLR EYTGPDGKRE IILCVANVSR AAQAAELDLS QYADSVPVEM LGGSAFPPIG
     QLPFLLTLAP YGFYWFLLAA KDQMPSWHVE PAQSLPEFTT LVLKKRMEEL LEAPARSTLQ
     DSILPQYLPK RRWFAGKEAG IEHVQIAYGV RFGTATYPVL LSEIEVTSAG QNSRYQLPFG
     FVGEDQITSA PPQQLALARV RRGRQVGLIT DGFVLESFIH AVLQACRDAV RLPCAEGELR
     FHATEQLAAL NLADDAQVRY LSAEQSNSSV VVGGSLVLKL IRRINPGVHP ELEMSAYLTA
     AGFGNISPLL GWVSRVDSQQ QAHLLMIAQG YLSNQGDAWD WTQNNLERAI RDELEPGSST
     QEGHTNALQD LTGFAAMLGQ RLGEMHLLLA APSKAPAFRA RPSTARDCQA WGKHIGAQLS
     RALELLQAHR AELDSDSQAL VDELVQQRQD LLATVATLST QAQGGLLMRV HGDLHLGQVL
     VVQGDAYLID FEGEPARPLE ERRARHSPYK DVSGVLRSFD YAAAMVLRSA SSVDLSDSAR
     QARQRVARRY LHQARHAFVE AYGLATAAMP HAWEHADGER AALELFSLEK AAYEILYEAE
     NRPSWLAVPL HGLYGLTSTW GES
//
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