ID A0A1D9H3Q6_9BURK Unreviewed; 1123 AA.
AC A0A1D9H3Q6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BKK79_20960 {ECO:0000313|EMBL:AOY94424.1};
OS Cupriavidus sp. USMAA2-4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=876364 {ECO:0000313|EMBL:AOY94424.1, ECO:0000313|Proteomes:UP000178101};
RN [1] {ECO:0000313|EMBL:AOY94424.1, ECO:0000313|Proteomes:UP000178101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USMAA2-4 {ECO:0000313|EMBL:AOY94424.1,
RC ECO:0000313|Proteomes:UP000178101};
RA Abdullah A.A.-A., Shafie N.A.H., Lau N.S.;
RT "Complete genome sequences of three Cupriavidus strains isolated from
RT various Malaysian environments.";
RL Submitted (OCT-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}.
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DR EMBL; CP017749; AOY94424.1; -; Genomic_DNA.
DR RefSeq; WP_071038660.1; NZ_CP017749.1.
DR AlphaFoldDB; A0A1D9H3Q6; -.
DR STRING; 876364.BKK79_20960; -.
DR KEGG; cuu:BKK79_20960; -.
DR Proteomes; UP000178101; Chromosome 2.
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:0016740; F:transferase activity; 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:UP000178101};
KW Transferase {ECO:0000313|EMBL:AOY94424.1}.
FT DOMAIN 27..434
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1123 AA; 126755 MW; DF0CD2EF8E116A05 CRC64;
MKRLSERAHS ALLNADPLWY KDAVIYQLHI KSFFDGNGDG VGDFSGLLAK LDYLVDLGVD
TVWLLPFYPS PRLDDGYDIA DYRNVHPEYG TLSEARRFIH AAHAHGIRVI TELVINHTSD
QHPWFQRSRR AKPGSAARNY YVWSDDDQAY AGTRIIFCDT EKSNWSWDPV AGAYFWHRFY
AHQPDLNFDN PHVLSEVLSV MRFWLDIGVD GLRLDAVPYL VEREGTSNEN LPETHAIIRK
IRAHLDARYP GRMLLAEANM WPEDAQQYFG IDGAAADGRG EECHMAFHFP LMPRMYMAIA
REDRFPITDI MRQTPEVPVD CQWAIFLRNH DELTLEMVTS SERDYLWEVY ASERRARINL
GIRRRLAPLM ERDRRRIELM NSLLFSMPGT PVIYYGDEIG MGDNIHLGDR DGVRTPMQWS
PDRNGGFSRA DPERLVLPPL QGPLYGYEAV NVEAQERDPH SLLNWMRRML ALRRKHRAFG
RGTLRFLFPG NRKILAYLRE YDDVHILCVA NLSRAPQAVE LDLSAFNGRV PVEMMGATPF
PAIGTLTYLL TLPPYGFYWF VLSDEAQPPP WHMETPEQMP DQVTLVLQNR GRPELTEASR
RLLDEEVLPP YLRRRRWFGA KGETIRRASL AYMLPFARGD GGEETWLGEV EVVLAGGRTE
RYQLPVGLLW DRDNPDGIPP LAHGLSMARV RQGSRVGLAT DGFTSELFAR EIVQALRAGS
ELRGPQETIR FKAEPGLAAM HPEREEIQWM SAEQSNSSLA YGNTAVLKLV RRLSGGCHPE
VEVTRYLTSQ GYPHCAPLLG EAVRIGADGE PHTLMLLQGY IPNQGNGWDW TLDYLARAID
DALPAKESED EFIEAMSGYA AMATTLGRRL AELHEVLARS SEDPAFAPEP AGAAKSEQWA
RQALARLTHA LDLLEICPID TSQPAQERLG EDVQLLLQAR QALPALVERL AAAAPGGLQT
RIHGDFHLGQ VLIAQNDAYL VDFEGEPGQP LAWRRRKTSP LRDVAGLLRS LDYAAATVGT
DRQERTHAEL PPALAQRRGE LLERFRATAT EAVLGGYREH LEACATPWVQ AGQLQPLLDL
FLLERAAYEV EYEAANRVAW IDLPASGLAR LVGQLLADDT EAR
//
