ID A0A0P0RGV6_9BURK Unreviewed; 1152 AA.
AC A0A0P0RGV6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=K788_0000987 {ECO:0000313|EMBL:ALL67897.1};
OS Paraburkholderia caribensis MBA4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1323664 {ECO:0000313|EMBL:ALL67897.1, ECO:0000313|Proteomes:UP000019146};
RN [1] {ECO:0000313|EMBL:ALL67897.1, ECO:0000313|Proteomes:UP000019146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBA4 {ECO:0000313|EMBL:ALL67897.1,
RC ECO:0000313|Proteomes:UP000019146};
RX PubMed=24558235;
RA Pan Y., Kong K.F., Tsang J.S.;
RT "Draft Genome Sequence of the Haloacid-Degrading Burkholderia caribensis
RT Strain MBA4.";
RL Genome Announc. 2:e00047-e00014(2014).
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; CP012747; ALL67897.1; -; Genomic_DNA.
DR RefSeq; WP_035999389.1; NZ_CP012747.1.
DR AlphaFoldDB; A0A0P0RGV6; -.
DR GeneID; 69971674; -.
DR KEGG; bcai:K788_0000987; -.
DR Proteomes; UP000019146; Chromosome 2.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000313|EMBL:ALL67897.1};
KW Hydrolase {ECO:0000313|EMBL:ALL67897.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ALL67897.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 51..464
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 842..876
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1152 AA; 129685 MW; 1884E6C68304B9E1 CRC64;
MKRDDPAEST SQHFTDTTAE AAPAKARPSR RARVSTLADD PLWYKDAIIY QVHIKSFFDA
NNDGVGDFPG LIAKLDYIAE LGVSAIWLLP FYPSPRRDDG YDIADYKSVH PDYGTIGDVK
RFIQEAHARG LHVITELVIN HTSDQHPWFQ RARRAKPGSN HRNYYVWSDT DKKYEQTRII
FIDSEPSNWT HDPVAGQYYW HRFYAHQPDL NFDNPAVLRE VLQVMRFWLD LGIDGLRLDA
VPYLVEREGT NNENLPETHA ILKKIRATID AEYPNRMLLA EANQWPEDVQ EYFGNEDECH
MAFHFPLMPR IYMSIASEDR FPITDIMKQT PDLPETNQWA IFLRNHDELT LEMVTDSERD
YLWNTYASDR RARLNLGIRR RLAPLMERDR RRIELINSLL LSMPGTPVIY YGDELGMGDN
IHLGDRDGVR TPMQWSSDRN GGFSRADPEQ LVLPPVMGSL YGFDAVNVEA QSRDPHSLLN
WTRRMLATRR SKHTFGRGTI RFLKPSNRKI LAYLRELPGE PPILCVANLS RAPQAVELDL
SEFNGAVPIE MTADSVFPRI GQLTYLLTFP PYGFLWFLLC EGGGRPTWSQ APSEPLPDFV
TIVIREGQAG PTPENVRLLE SEVLPSWLGR RRWFASKDQK MHAVRLAALT TIPEAGFAFT
EIEADVGNHT ERYVLPLAIT WGADTTTPLF MQLALARVRR GRNVGHLTDA FSLPQFAYGT
LRKLRERAGV PTVQKSTIHF IPTDRFNELD LGDQPEIRWL AAEQSNSSLV IADKVVLKLV
RRLLKGMHPE AEMSRYLTQL GYANTAPLYG EVVRVDPENV PHTLCILQGF VDNQGDAWNW
ALDTLRRSID ELALAVDGAS NENQANQDRV NEEEATEGYA SYMGIIGKRL GELHVALATP
SDNPAFDPEP ADSKQVQAWI DGTQKLLATA LELLEKNVDQ LGEDAALLGR SVLDRKDKLV
EAVSKLVKPD AHALRTRIHG DFHLGQVLVA QGDAFLIDFE GEPARELEER RAKSSPLRDV
AGLLRSLSYA SAAAQSTMEA APQMTADRKR ALFERFRAAA AEAFLTEYRA ATQAAPQRLV
APEHEQALLD LFLIEKAAYE IRYEAANRPA WLGLPVRGLA ALTSRLLGDT GAAPHSPAAA
SAPPAASEGD YE
//