ID A0A177QX78_9PROT Unreviewed; 1079 AA.
AC A0A177QX78;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=AYO46_08685 {ECO:0000313|EMBL:OAI51143.1};
OS Betaproteobacteria bacterium SCGC AG-212-J23.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1799662 {ECO:0000313|EMBL:OAI51143.1, ECO:0000313|Proteomes:UP000077532};
RN [1] {ECO:0000313|Proteomes:UP000077532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-J23 {ECO:0000313|Proteomes:UP000077532};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAI51143.1}.
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DR EMBL; LSTF01000067; OAI51143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177QX78; -.
DR Proteomes; UP000077532; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077532}.
FT DOMAIN 37..436
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1079 AA; 123544 MW; A175CCE2ACA418A9 CRC64;
MSSVLSEDKE IREVAEADKE QSSTDRALWY KDAVIYQLHV KAFMDSNGDG IGDFAGLASK
LDYIQELGVN AVWLLPFYPS PLKDDGYDVA DYRNVHPHYG TREDFRKFVD EAHRRGLKVI
TELVVNHTSD QHPWFQAARR APPGSRKRDY YVWSDTETKY RGTRIIFTDT ETSNWAWDPV
AKQYYWHRFF SHQPDLNFDN PHVVRAVLKV MQSWAEMGVD GFRLDAIPYL CEREGTTNEN
LPETHLVLKQ IRAAISARYP GRMLLAEANM WPEDVRPYFG DSDECHMAFH FPLMPRMYMA
IAQEDRHPLV EIMQQTPEIP DICQWAIFLR NHDELTLEMV TSRERDYMYR MYAADRQARI
NLGIRRRLAP LMENDPERIK LMNSLLLSMP GSPILYYGDE LGMGDNIYLG DRNGVRTPMQ
WSPDRNAGFS KADPQRLYLP PIMDPIYGYE AVNVEAQQRD PNSLLNWTKR MLAIRKTSHA
FGRGKLSFLS PGNRKVLAYI RELNDEAILC VGNLSRAAQP VELDLKKYKG RIPVELLGRT
SFPPIGDLPY LLTLPAHGFY WFRLATDAKP PDWHTDQLVP DEMPLMVLFD GWTSFFRDKV
VPWRIRMAEE LRGELEAKVL PRFIEKQRWY AQKGEAVKRA EIRDHVVWDV GGVSWLLNFI
STNNSLYFLP LAFGWEEDED HMRALSATAI ARVRQQANVG IIADALADES LLRHIVKSVG
EGRTLKTEQG ELRFTPSASF AQIAGSEVTT LMPGALRAQS TNTSVVLGDR LFLKAYRRLR
PGLHPELEVG RYLTEVARFK HCVPLAGSVE YFSKEKESMT VALLQAYVPN QGDAWSYTLA
YLERFAEGKR TDDGHGGFLA LMQTLATRTA ELHLAFAAAK NDPAFTPEPL TTEDVDAWRA
RVREEASQTI ALVENIKPLG PQIMSFIAAC AAPKKRSLRT RHHGDYHLGQ VLVSNNDFLI
IDFEGEPSRP LAEARRKHSP LRDVAGMLRS FSYARGSVEI QEQVRELSEW ERQTRQAFVD
AYAKAAEGSG LYESFEDVQG LLRLAEMEKV LYELRYEKNN RPNWLHIPLQ GLTALLQGD
//
