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
//