ID TREY_ARTSQ Reviewed; 775 AA. AC Q44315; DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-SEP-2023, entry version 96. DE RecName: Full=Maltooligosyl trehalose synthase; DE EC=5.4.99.15; DE AltName: Full=(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase; GN Name=treY; OS Arthrobacter sp. (strain Q36). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Arthrobacter. OX NCBI_TaxID=104027; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8605217; DOI=10.1016/0304-4165(95)00139-5; RA Maruta K., Hattori K., Nakada T., Kubota M., Sugimoto T., Kurimoto M.; RT "Cloning and sequencing of trehalose biosynthesis genes from Arthrobacter RT sp. Q36."; RL Biochim. Biophys. Acta 1289:10-13(1996). RN [2] RP CHARACTERIZATION. RX PubMed=8611744; DOI=10.1271/bbb.59.2210; RA Nakada T., Maruta K., Tsusaki K., Kubota M., Chaen H., Sugimoto T., RA Kurimoto M., Tsujisaka Y.; RT "Purification and properties of a novel enzyme, maltooligosyl trehalose RT synthase, from Arthrobacter sp. Q36."; RL Biosci. Biotechnol. Biochem. 59:2210-2214(1995). CC -!- FUNCTION: Catalyzes the conversion of maltooligosaccharide into the CC non-reducing saccharide, maltooligosyl trehalose (alpha-maltooligosyl CC alpha-D-glucoside) by intramolecular transglycosylation. CC -!- CATALYTIC ACTIVITY: CC Reaction=4-[(1->4)-alpha-D-glucosyl](n-1)-D-glucose = 1-[(1->4)-alpha- CC D-glucosyl](n-1)-alpha-D-glucose; Xref=Rhea:RHEA:13621, Rhea:RHEA- CC COMP:14708, Rhea:RHEA-COMP:14709, ChEBI:CHEBI:140774, CC ChEBI:CHEBI:140775; EC=5.4.99.15; CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}. 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; D63343; BAA09667.1; -; Genomic_DNA. DR PIR; S65769; S65769. DR AlphaFoldDB; Q44315; -. DR SMR; Q44315; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR KEGG; ag:BAA09667; -. DR BioCyc; MetaCyc:MONOMER-6021; -. DR GO; GO:0047470; F:(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11336; AmyAc_MTSase; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 3.30.1590.10; Maltooligosyl trehalose synthase, domain 2; 1. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013797; Maltooligo_trehalose_synth_4. DR InterPro; IPR012767; Trehalose_TreY. DR NCBIfam; TIGR02401; trehalose_TreY; 1. DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1. DR PANTHER; PTHR10357:SF216; MALTOOLIGOSYL TREHALOSE SYNTHASE-RELATED; 1. DR Pfam; PF00128; Alpha-amylase; 1. DR SMART; SM00642; Aamy; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW Isomerase. FT CHAIN 1..775 FT /note="Maltooligosyl trehalose synthase" FT /id="PRO_0000054341" SQ SEQUENCE 775 AA; 85356 MW; 1BBD23024B2280FC CRC64; MRTPVSTYRL QIRKGFTLFD AAKTVPYLHS LGVDWVYLSP VLTAEQGSDH GYDVTDPSAV DPERGGPEGL AAVSKAARAA GMGVLIDIVP NHVGVATPAQ NPWWWSLLKE GRQSRYAEAF DVDWDLAGGR IRLPVLGSDD DLDQLEIRDG ELRYYDHRFP LAEGTYAEGD APRDVHARQH YELIGWRRAD NELNYRRFFA VNTLAGVRVE IPAVFDEAHQ EVVRWFREDL ADGLRIDHPD GLADPEGYLK RLREVTGGAY LLIEKILEPG EQLPASFECE GTTGYDALAD VDRVLVDPRG QEPLDRLDAS LRGGEPADYQ DMIRGTKRRI TDGILHSEIL RLARLVPGDA NVSIDAGADA LAEIIAAFPV YRTYLPEGAE VLKEACELAA RRRPELDQAI QALQPLLLDT DLELARRFQQ TSGMVMAKGV EDTAFFRYNR LGTLTEVGAD PTEFAVEPDE FHARLARRQA ELPLSMTTLS THDTKRSEDT RARISVISEV AGDWEKALNR LRDLAPLPDG PLSALLWQAI AGAWPASRER LQYYALKAAR EAGNSTNWTD PAPAFEEKLK AAVDAVFDNP AVQAEVEALV ELLEPYGASN SLAAKLVQLT MPGVPDVYQG TEFWDRSLTD PDNRRPFSFD DRRAALEQLD AGDLPASFTD ERTKLLVTSR ALRLRRDRPE LFTGYRPVLA SGPAAGHLLA FDRGTAAAPG ALTLATRLPY GLEQSGGWRD TAVELNTAMK DELTGAGFGP GAVKIADIFR SFPVALLVPQ TGGES //