ID A0A0G3BDX4_9BURK Unreviewed; 1113 AA.
AC A0A0G3BDX4;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:AKJ27492.1};
GN ORFNames=AAW51_0801 {ECO:0000313|EMBL:AKJ27492.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ27492.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ27492.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ27492.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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; CP011371; AKJ27492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3BDX4; -.
DR STRING; 413882.AAW51_0801; -.
DR KEGG; pbh:AAW51_0801; -.
DR PATRIC; fig|413882.6.peg.848; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000035352; 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; IPR002575; Aminoglycoside_PTrfase.
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; PF01636; APH; 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:UP000035352}.
FT DOMAIN 35..434
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1113 AA; 128531 MW; B200018786B791EC CRC64;
MMNTAPTHSA VPGHIVSASP DLDEALWYKD AVIYQVNVKA FYDSNDDGIG DFKGLTSKLD
YIKELGVNTI WLMPFYPSPL RDDGYDISDY HNVHPMYGTR HDFRIFLREA HRRGLKVITE
LVINHTSDTH PWFQAARRAP PGSIKRDYYV WSDDDQKYKG TRIIFTDTET SNWTWDPVAK
AYYWHRFFSH QPDLNFDNPH VLKAVFRTMR FWLDMGVDGF RLDAIPYLIE RDGTNNENLP
ETHQIIKQLR AAIDARYKNR FLLAEANQWP EDVREYFGNG DECHMCYHFP LMPRIYMSIA
QEDRYPIIEI MQQTPEIPET CQWAIFLRNH DELTLEMVTS KERDYMYNTY AADPRARINL
GIRRRLAPLM ENDPDRVKLM NSLLLSMPGS PIIYYGDEIG MGDNVFVGDR NGVRTPMQWS
PDRNAGFSRA DPQRLYLPPI MDPVYGFQAV NVEAQSRAPS SLLNWTRRML AVRNTSKAFG
RGRRTYLKPG NRKILAYLSE YADDVILCVA NMSRTAQPVE LDLARFKGRV PVEMLGRVTF
PPIGDLPYLL TLPAYGFYWF KLTVDAEMPQ WHDERLPRDD RPVLVLFDGW NSLFRDQVVP
WRIGLAEKTR AQFEHEAVPR YLETQRWYAT KGDEVKRAAL CDHAFWREGD TSWLLPLFEL
EGPQERSRYF MPLALAWEDH DEERLPNLVP AMVAKVRQQA NVGVLADAFC DEAFCRAMVT
AIGAGRELAT ARGKLYFKPT SAFGEIAGAD LSKLPVGRPS AQSTNTVVTL DERLFLKGYR
RIRPGVNLEF EVGRYLTEVV RYPNCVPVAG ALEYVDHNGT ISTLALVQAY VSNQGDGWDY
TTAYLQRFLD ERRTLDEPLP PDVHGAYMEL MHTLGRRTAE LHVAFARPSN DPAFNPEPLR
REDVDTWRHQ ALEETRETFE LLEANVSHLP QTALGEAKTL MARREQVTAR IESCLRELPE
QVLKTRYHGD YHLGQVLLTK NDFVIIDFEG EPARSFEERR AKHSSLRDVA GLLRSFNYAH
WEGLRRVAET PEQFERLAPL ARAWEAESRA AFLRSYEETA RESGLYTSLA SVRGLLELFE
LEKALYELRY ELRNRPDWVS IPLQGILGLA ERP
//
