ID F8CC48_MYXFH Unreviewed; 551 AA. AC F8CC48; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 59. DE RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619}; DE EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619}; DE AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378}; GN OrderedLocusNames=LILAB_26565 {ECO:0000313|EMBL:AEI67205.1}; OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Myxococcaceae; Myxococcus. OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI67205.1, ECO:0000313|Proteomes:UP000000488}; RN [1] {ECO:0000313|EMBL:AEI67205.1, ECO:0000313|Proteomes:UP000000488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488}; RX PubMed=21868801; DOI=10.1128/JB.05516-11; RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.; RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW- RT 1."; RL J. Bacteriol. 193:5015-5016(2011). 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 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; CP002830; AEI67205.1; -; Genomic_DNA. DR AlphaFoldDB; F8CC48; -. DR STRING; 483219.LILAB_26565; -. DR KEGG; mfu:LILAB_26565; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_006462_2_1_7; -. DR Proteomes; UP000000488; 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; 3.20.20.80; 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; IPR032091; Malt_amylase_C. DR InterPro; IPR045857; O16G_dom_2. DR InterPro; IPR012810; TreS/a-amylase_N. 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; PF16657; Malt_amylase_C; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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}. FT DOMAIN 15..413 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 551 AA; 65205 MW; 51FB5BA14957E88A CRC64; MDLDPLWYKK ALIYELHLRA FHDSNGDGHG DIPGLIEKLP YLQDLGVNCL WLLPHYPSPL RDDGYDIADY YGVHPDYGTL ADFQRLVDEA HKRDIRIITE LVVNHTSDQH PWFQEARSDP NSPKRDWYVW SDTDEQYKGA RIIFLDTERS NWTWDPVAKQ YFWHRFFSHQ PDLNYDNPEV QEAMLDVMRF WLNMGVDGFR CDAVPYLFER EDTNCENLPE THAFLKRLRK TIDAEYQGKM LLAEANQWPA DVRVYFGDGD EFHMGFHFPV MPRLFMAVRR EDRTPIVEIM QQTPDIPDNC QWAIFLRNHD ELTLEMVTDE DRDYMYREYA TDPRMRINLG IRRRLAPLMD NGRRRIELMH SLLFTLPGTP VLYYGDEIGM GDNIYLGDRN GVRTPMQWTG DRNAGFSRAD YSRLYAPVIA DPVYGYQSIN VEAQERVKSS LLHWVKRMIR IRQRYPVFSL GNLRFLQTDN RKVLAFIREW EGQTVLVVCN LSRFAQPAVL DMREWEGTVP VELIGETPFP RVSELPYQLS MGPYMFLWFR LDRPQQERSL E //