ID Q3STC1_NITWN Unreviewed; 1094 AA. AC Q3STC1; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 110. 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=Nwi_1208 {ECO:0000313|EMBL:ABA04470.1}; OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / OS NCIMB 11846 / Nb-255). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Nitrobacter. OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA04470.1, ECO:0000313|Proteomes:UP000002531}; RN [1] {ECO:0000313|EMBL:ABA04470.1, ECO:0000313|Proteomes:UP000002531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255 RC {ECO:0000313|Proteomes:UP000002531}; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L., RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., RA Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium RT Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). 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; CP000115; ABA04470.1; -; Genomic_DNA. DR RefSeq; WP_011314499.1; NC_007406.1. DR AlphaFoldDB; Q3STC1; -. DR STRING; 323098.Nwi_1208; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; nwi:Nwi_1208; -. DR eggNOG; COG0366; Bacteria. DR eggNOG; COG3281; Bacteria. DR HOGENOM; CLU_007635_1_2_5; -. DR OrthoDB; 9805159at2; -. DR Proteomes; UP000002531; 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; 3.90.1200.10; -; 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; 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; 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, ECO:0000313|EMBL:ABA04470.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000002531}. FT DOMAIN 27..426 FT /note="Glycosyl hydrolase family 13 catalytic" FT /evidence="ECO:0000259|SMART:SM00642" SQ SEQUENCE 1094 AA; 124586 MW; 8EA29E353D0B3A97 CRC64; MNEMSHIDAD RYVQTDDLWY KDAIIYQLHV KAFADSNNDG IGDFVGLTNK LDYLQELGVT ALWLLPFYPS PGRDDGYDIA DYGSVNPDFG TMKDFRRFIS EAKRRGLRVI TELVINHTSD QHRWFKRAQR SPAGSSARNW YVWSNTDKKY QGTRIIFTDT EKSNWAWDSE ANAYYWHRFF SHQPDLNFDN PRVVRAVIQV MKRWLDTGVD GFRLDAIPYL CEREGTNNEN LPETHAVIKH IRAALDSYAK GKVLLAEANQ WPEDVQFYFG DGDECHMAYH FPLMPRIYMA IAQEDRFPIT DILRQTPDIP DNCQWAMFLR NHDELTLEMV TDIERDYLWS TYAADPRARI NLGIRRRLAP LMDNDRRKIE LMNSLLMSLP GTPIIYYGDE IGMGDNIYLG DRNGVRTPMQ WTSDRNGGFS RCDPARLYAP PVMDAVYGYE SVNVESQSRS LSSLLSWMKK LISVRKSSHV FGRGTMAFVR SSNRSVLAYL RQHGDEAVLC VANLSRSAQA SELDLSHWKG RSPLEMLGRT TFPDIGELPY LITLAPYGFY WFRLNEKPPS PNVAAVIVPD YETLVVPQGA TWMSLARTRS IFERDVLPSH LARSRWFPER SAGAITARVP AAIPLTKDQV SRPWLSIFDV THRGQTGRYA MPIQIRWDRL DRKNYDARNV AAVRQGSREG TLIDAAYESG LITGIIEGLR QRATFEGGNL QISYIPTERL ASITEEPIEN VRPVQTEQSN STALVDQKFV VKLYRKLENG INPEVEVGRF LTDVAGYANT PALLGSVELT GPDVHAAVAI VHAFVGNQGD AWTISSAALD RFIDEQRLVG AIDTAPALEE KAAYQRYMMQ LGKRVAEMHV ALASRGDIED FRPEPVNASD VAHFIDRLTA RAEKTFDRLA QARLSESDRI LVEEIQSLRP ALHGLLAGLL PSSIQMYSIR HHGDFHLGQV LVVRDDVFII DFEGEPRRSL SERRMKAPAA RDVAGLIRSI DYSVTSAQQR VLKTEVDDDG RLAEALSAWR DEATQTFLIA YREAMSDSRL WPQDNDESEG MLRFFLLEKA LYEIDYELAH RPDWLRVALD GALRVLRNDK RDRA //