ID A7HEM1_ANADF Unreviewed; 553 AA. AC A7HEM1; DT 11-SEP-2007, integrated into UniProtKB/TrEMBL. DT 11-SEP-2007, sequence version 1. DT 27-MAR-2024, entry version 78. 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=Anae109_2968 {ECO:0000313|EMBL:ABS27167.1}; OS Anaeromyxobacter sp. (strain Fw109-5). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27167.1, ECO:0000313|Proteomes:UP000006382}; RN [1] {ECO:0000313|EMBL:ABS27167.1, ECO:0000313|Proteomes:UP000006382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27167.1, RC ECO:0000313|Proteomes:UP000006382}; RX PubMed=25614562; DOI=10.1128/genomeA.01449-14; RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T., RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C., RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J., RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A., RA Loeffler F.E., Fields M.W.; RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic, RT metal-reducing bacterium isolated from a contaminated subsurface RT environment."; RL Genome Announc. 3:0-0(2015). 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; CP000769; ABS27167.1; -; Genomic_DNA. DR RefSeq; WP_012097776.1; NC_009675.1. DR AlphaFoldDB; A7HEM1; -. DR STRING; 404589.Anae109_2968; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; afw:Anae109_2968; -. DR eggNOG; COG0366; Bacteria. DR HOGENOM; CLU_006462_2_1_7; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000006382; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000006382}. FT DOMAIN 22..421 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 553 AA; 64567 MW; 75A3BFEF9FA0BFAF CRC64; MASFQRRRGQ DPLWYKDAVI YETHVKTFYD SNGDGIGDLR GLVEKLDYLQ DLGINCLWLL PLFPSPLKDD GYDIADYRGI HPDYGTMDDF RELVAAAHAR GIRVLIELVV NHTSDQHPWF QRARRAPPGS PERAFYVWSD TDQKYPDARI IFTDTEKSNW TWDPEAKQYY WHRFFSHQPD LNFENPQVLR EVLDALSFWA ELGVDAFRLD AVPYLIEQDG TNCENLPRTH EVIKQVRRHV DEHFPGRMLL AEANQWPDDV RPYFGEGDEC HMAFHFPLMP RIFMALRLED VEPIVEIMRR TPPIPDTSQW ALFLRNHDEL TLEMVTNDER DYMYLAYGHD PRMKLNVGIR RRLMPLVENS RRRMELLNSL LFSFPGTPVV YYGDEIGMGD NIYLHDRNGV RTPMQWTPDR NAGFSRADPG RLYSAPISDP VYGYQAVNVE GQSRDPSSLL HWMRNTIALR KLFKAFGRGT MEFLPVANRK VLAYVRRWEE DVILCVANVS RSAQPAELDL SALEGYVPVE MLGYTEFPRI GKLPYFLTLG PYGFYWFELR KPH //