ID B7KQL5_METC4 Unreviewed; 1088 AA. AC B7KQL5; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 83. 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=Mchl_2940 {ECO:0000313|EMBL:ACK83779.1}; OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium OS extorquens). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Methylobacteriaceae; Methylorubrum. OX NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK83779.1, ECO:0000313|Proteomes:UP000002385}; RN [1] {ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Marx C., Richardson P.; RT "Complete sequence of chromosome of Methylobacterium chloromethanicum RT CM4."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACK83779.1, ECO:0000313|Proteomes:UP000002385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385}; RX PubMed=22887658; DOI=10.1128/JB.01009-12; RA Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M., RA Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E., RA Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N., RA Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M., RA Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.; RT "Complete genome sequences of six strains of the genus Methylobacterium."; RL J. Bacteriol. 194:4746-4748(2012). 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; CP001298; ACK83779.1; -; Genomic_DNA. DR RefSeq; WP_015951201.1; NC_011757.1. DR AlphaFoldDB; B7KQL5; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; mch:Mchl_2940; -. DR HOGENOM; CLU_007635_1_1_5; -. DR Proteomes; UP000002385; Chromosome. DR GO; GO:0016301; F:kinase activity; 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:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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 Kinase {ECO:0000256|ARBA:ARBA00022777}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Transferase {ECO:0000256|ARBA:ARBA00022777}. FT DOMAIN 17..411 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 1088 AA; 122104 MW; 5A82AB8B73873E72 CRC64; MIDRSDPQWY RDAIIYQIHV KSFFDSSNDG IGDFEGLTQK LDYVRDLGVT AIWLMPFYPS PLRDDGYDIA DYRDVNPSYG TMEDFRRFVA AAHERGLRVI TELVINHTSD QHPWFQRARE APAGSPERDF YVWSDTDEKY SDTRIIFLDT EVSNWTWDPV AKQYFWHRFY SHQPDLNFDN PAVLEAVIEV MRYWLDMGVD GLRLDAIPYL IERDGTNCEN LSETHDVIKA IRAALDAEYP DRMLLAEANQ WPEETAQYFG EGDECHMAFH FPLMPRMYMA IAREDRHPIT DIMRQTPEIP EGCQWAIFLR NHDELTLEMV TAEERDYLWS FYAAERRARI NLGIRRRLAP LLENDRRKIE LMKSLVLSMP GTPVLYYGDE IGMGDNIYLG DRDGVRTPMQ WSPDRNGGFS RATPQKLFLP SIQDPIYGYD AINVEAQIQA QTSLLNWTRR MIAIRNNSVA LGRGAIQFLY PANRKVLAWI REHENERILC VANLSRAPQA VQLDLSDLRG AIPIELTGGT AFPAIGELPY LLTLPAYGFY WFALSVANTG EIGPQPQSPE LFTLVLTGGI ETLIKGRERT AFERTVAPPF IASRRWFGAK GTRIKSVQVD DSAIVKDGSG EGKFLLPRVA VTLANGERQD YFVPLAVEEG REDETLLGHA VARVRRGPRT GLLYEAAAAA PFAVALIEAM RDGVTIPSER GSLVFSTTSA YDPEVPFEAA DVRRLSAEQS NTSIAIGARM MLKLLRRLQP GTHPEIEIGR FLTEQAHFAN TPALLGVVEH VAADGTRTAL ALLQKFVLNQ GDAWTLMLEG LRRDFETVVL APESEAPAPE DAFNAHLRWA ELLGQRTAEL HRAFAIDTDD PAFAVEPFDE ADLASLADDA RHQAARAFKG LDAITAWSPG SASEALASRR SEVEALITDL ASGPLRGATK TRIHGDYHLG QVLASEGDLI IVDFEGEPSR PVEQRRAKST PMRDVAGMLR SFAYGAETVV REITARFGDS EERARNAAIA WRGMIDAAFL DGYGQAVAGS RAAVEDAETQ SRLLRLSLLT KALYEVDYEV NNRPDWIEIP ARGVLNILDE AKRDRASV //