ID A0A3N6MPM5_9BURK Unreviewed; 1153 AA.
AC A0A3N6MPM5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 Name=treS {ECO:0000313|EMBL:RQH05679.1};
GN ORFNames=D1Y85_13670 {ECO:0000313|EMBL:RQH05679.1};
OS Paraburkholderia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH05679.1, ECO:0000313|Proteomes:UP000272778};
RN [1] {ECO:0000313|EMBL:RQH05679.1, ECO:0000313|Proteomes:UP000272778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOA04 {ECO:0000313|EMBL:RQH05679.1,
RC ECO:0000313|Proteomes:UP000272778};
RA Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT "Paraburkholderia sp. DHOA04, isolated from soil.";
RL Submitted (NOV-2018) 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:RQH05679.1}.
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DR EMBL; RQIS01000009; RQH05679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N6MPM5; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000272778; 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: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, ECO:0000313|EMBL:RQH05679.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000272778};
KW Transferase {ECO:0000313|EMBL:RQH05679.1}.
FT DOMAIN 57..451
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 129505 MW; 8694AA8B2775B58A CRC64;
MKRDSPTHAP SAREVTHDST APGEPGEAGG LAATQRRGKP SFLSDDPLWY KDAVIYQVHV
KSFYDANNDG VGDFPGLLAK LDYIAGLGVT AIWLLPFYPS PRRDDGYDIA DYRNVHPDYG
QLADVRRFIQ EAHARGIRVI TELVINHTSD QHPWFQRARR SRPGSNHRNY YVWSDTDAKY
AGTRIIFIDT EPSNWTHDPV AGAYYWHRFY SHQPDLNFDN PAVLREVLQI MRFWLDMGID
GLRLDAVPYL VEREGTNNEN LPETHEILKQ IRKAIDTHYP NRMLLAEANQ WPEDVQEYFG
NEDECHMAFH FPLMPRLYMA IASEDRFPII DIMKQTPDLP PSCQWAVFLR NHDELTLEMV
TDSERDYLWN TYASDRRARL NLGIRRRLAP LMERDRRRIE LINSLLLSMP GTPVIYYGDE
LGMGDNIHLG DRDGVRTPMQ WSSDRNGGFS RADPEQLVLP PLMGSLYGYD AINVEAQNRD
PHSLLNWTRR MLSTRRGKQT FGRGTIRFLR PENRKILAYL REMPGEPAIL CVANLSRAPQ
AVELDLSDYI GTSPVEMTAD SVFPPIGQLP YLLTFPPYGF LWFLLCPGTQ RPAWSQPTSE
QLPEFVTVVI REGQLGPTPE NVRLLESEVL PSWLSRRRWF ASKDRSLKGV RLAALTTIQG
AGFAFTEVEA EFRDGTSARY VLPIAISWGT ETTTPLHIQL ALSRVRRGRN VGYLTDAFSL
PWFAHGVLRK LREHAAVPTV QQSVIHFLPT ARLETLDPGE TPEIRWLAAE QSNSSLVIAD
MLVLKLVRRL MPGVHPEVEM SRYLTKLGYA NTAPLVGEVV RVDPQGVPHT LAILQGYVDN
QGNAWDWALD YLRRMTDELA HSGGDDEAAA DRAQEEEAEQ GYCTVIGAIG KRLGELHAAL
ATQTDDKAFA PEEATRADVR GWIADTKAML TEALDILARQ TATDLHPLDD DARELALGLL
ARRDALIAAV EHRVPPDVSA WRIRIHGDFH LGQVLLSQGD AYLIDFEGEP ARTLEYRRAK
ACPLRDVAGL LRSLSYAAAA AQSTTESAPQ QTADRKRTLF ERFRGYAAEA FLSHYRAAVA
DAPYALVSAS HEQDLLDLFL IEKAAYEIRY EAANRPTWLA LPVRGLAAIA GRVLGSTGAP
GTSGTPPAGG THG
//
