ID S4ZJD3_MYCIT Unreviewed; 593 AA. AC S4ZJD3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 27-MAR-2024, entry version 45. 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 ORFNames=OEM_50350 {ECO:0000313|EMBL:AGP66570.1}; OS Mycobacterium intracellulare subsp. yongonense 05-1390. OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=1138871 {ECO:0000313|EMBL:AGP66570.1, ECO:0000313|Proteomes:UP000014801}; RN [1] {ECO:0000313|EMBL:AGP66570.1, ECO:0000313|Proteomes:UP000014801} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=05-1390 {ECO:0000313|EMBL:AGP66570.1, RC ECO:0000313|Proteomes:UP000014801}; RX PubMed=23929490; RA Kim B.J., Kim B.R., Lee S.Y., Seok S.H., Kook Y.H., Kim B.J.; RT "Whole-Genome Sequence of a Novel Species, Mycobacterium yongonense DSM RT 45126T."; RL Genome Announc. 1:e00604-13(2013). 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; CP003347; AGP66570.1; -; Genomic_DNA. DR AlphaFoldDB; S4ZJD3; -. DR KEGG; myo:OEM_50350; -. DR PATRIC; fig|1138871.3.peg.5012; -. DR HOGENOM; CLU_006462_2_1_11; -. DR Proteomes; UP000014801; 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 54..456 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 593 AA; 67826 MW; ECF4CC4D4DF3C086 CRC64; MDLMNDAKEA VEHHPEGGSH VQDGVVEHPD AEDFNNAAAL PTDPTWFKHA VFYEVLVRAF FDANADGAGD LRGLLGQLDY LQWLGIDCIW LPPFYDSPLR DGGYDIRDFY KVLPEFGTVE DFVALLNAAH ERGIRVITDL VMNHTSDSHP WFQESRHDPD GPYGDYYVWS DTSERYTDAR IIFIDTEESN WTFDPVRKQF YWHRFFSHQP DLNYENPAVQ EAMIDVLRFW LGLGIDGFRL DAVPYLFERE GTNCENLPET HAFLKRVRKV VDDEFPGRVL LAEANQWPAD VVEYFGDPST GGDECHMAFH FPLMPRIFMA VRRESRFPIS EILAQTPEIP DMAQWGIFLR NHDELTLEMV TDEERDYMYS EYAKDPRMKA NVGIRRRLAP LLDNDRNQIE LFTALLLSLP GSPVLYYGDE IGMGDVIWLG DRDGVRTPMQ WTPDRNAGFS KANPGRLYLP PSQDSVYGYQ AVNVEAQRDT STSLLNFTRT MLAVRRRHEA FAIGSFEELG GSNPSVLAFL RQVSGDGDTV LCVNNLSRFP QPIELNLQHW SGCTPVELTG QVEFPRIGHL PYLLTLPGHG FYWFRLSGCE EDA //