ID C5AJ28_BURGB Unreviewed; 1151 AA. AC C5AJ28; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 78. 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 OrderedLocusNames=bglu_2g15560 {ECO:0000313|EMBL:ACR31908.1}; OS Burkholderia glumae (strain BGR1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR31908.1, ECO:0000313|Proteomes:UP000002187}; RN [1] {ECO:0000313|EMBL:ACR31908.1, ECO:0000313|Proteomes:UP000002187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR31908.1, RC ECO:0000313|Proteomes:UP000002187}; RX PubMed=19329631; DOI=10.1128/JB.00349-09; RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.; RT "Complete genome sequence of Burkholderia glumae BGR1."; RL J. Bacteriol. 191:3758-3759(2009). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001504; ACR31908.1; -; Genomic_DNA. DR RefSeq; WP_015877601.1; NC_012721.2. DR AlphaFoldDB; C5AJ28; -. DR STRING; 626418.bglu_2g15560; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GeneID; 58139138; -. DR KEGG; bgl:bglu_2g15560; -. DR PATRIC; fig|626418.3.peg.1849; -. DR eggNOG; COG0366; Bacteria. DR eggNOG; COG3281; Bacteria. DR HOGENOM; CLU_007635_0_0_4; -. DR Proteomes; UP000002187; 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: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:UP000002187}. FT DOMAIN 54..448 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT REGION 1..40 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1151 AA; 127338 MW; 2135C81C527CCCF6 CRC64; MIREEPLDQL PHAPFQPAAG SPRRGARRAG ASRAAGPGAA PADPLWYKDA IIYQLHVKSF FDSNGDGIGD FPGLISKLDY IASLGVDALW LLPFYPSPRR DDGYDIADYR NVHPDYGTLA DVRRFIREAH ARGIRVITEL VINHTSDQHP WFQRARRAKP GSVHRDYYVW SDTDTKFAGT RIIFVDSEPS NWTHDPVAGQ YYWHRFYSHQ PDLNFDNPAV VREVLQVMRF WLDLGIDGLR LDAVPYLVER EGTSNENLPE THAILKTIRA AIDAEYPNRM LLAEANQWPE DVQEYFGDED ECHMAFHFPL MPRIYMSIAS EDRFPIIDIM RQTPELAPSN QWAIFLRNHD ELTLEMVTDS ERDLLWQTYA ADRRARLNLG IRRRLAPLME RDRRRIELIN SLLLSMPGTP VIYYGDELGM GDNIHLGDRD GVRTPMQWSA DRNGGFSRAD PEQLVLPPVM GALYGYDAVN VEAQSRDPHS LLNWMRRILA TRRATQVFGR GTLRFLRPEN RKILAYLREL PDATPVLCVA NLSRASQAVE LDLSEFAGCV PVEMTSDSPF PAIGELPYLL TFPPYGFLWF QLSASGAEPA WHRPHAEPLP EFTTLVMRRG DTHPAAALVA TLEAEVLPSW LTRRRWFASK DRALQAVRFE CVTPVPGEAF QYAELVATVD GREDRYAVPL AAAWGDETSH PLFMRLALAR VRRGPTVGYL TDAFALPCFA HGVLRRLADP RDVPLAAGGT LVFSPEPAPA LAQYALGDAP EVRWLAAEQS NSSLVIGEAL VLKLVRRVAP GIHPEAEVSR HLTRAGYRNA PALVGEVRRV APDGTPHTVA IVQNFVDNQG DAWARALDFL KRAVSDLALA AAATPEAEAG ESAQAALELD TYAAFAGAIG KRLGELHVVL AAPSDDPAFA PERATPAHVE GWTADALAMF ERAAALLAPR LDELDADARE AAAALLASRE AIAQAIGTLV PRELGATCMR IHGDFHLGQV LEVNGDAMLI DFEGEPARPL AARRAKSHPL RDVAGLLRSL SYASAAAQFA IEKAPAPTAD LKRALFDRFG QAAADRFLAS YREACEAAAE PFVAAEHGER LLMLFLIEKA SYELGYEAAN RPDWLRVPVV GLASLAAQLL GRPLAAPPRS PDHPAAPEKK P //