ID   A1R391_PAEAT            Unreviewed;       598 AA.
AC   A1R391;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 108.
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   Name=treS {ECO:0000313|EMBL:ABM10189.1};
GN   OrderedLocusNames=AAur_0909 {ECO:0000313|EMBL:ABM10189.1};
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Paenarthrobacter.
OX   NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM10189.1, ECO:0000313|Proteomes:UP000000637};
RN   [1] {ECO:0000313|EMBL:ABM10189.1, ECO:0000313|Proteomes:UP000000637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:ABM10189.1,
RC   ECO:0000313|Proteomes:UP000000637};
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA   Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(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}.
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DR   EMBL; CP000474; ABM10189.1; -; Genomic_DNA.
DR   RefSeq; WP_011773650.1; NC_008711.1.
DR   AlphaFoldDB; A1R391; -.
DR   STRING; 290340.AAur_0909; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; aau:AAur_0909; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000000637; 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, ECO:0000313|EMBL:ABM10189.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          39..439
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   598 AA;  68042 MW;  8E5F8E8B123BB434 CRC64;
     MSFSPQNPSQ YFTPKNTFEL NAPGLQHDPH WYRKAVFYEV LVRAFADANG DGSGDFHGLI
     EKLDYLQWLG VDCLWLPPFF HSPLRDGGYD IADYTSVLDE FGTISDFKRL VAEAHARGVR
     VIIDLPLNHT SDQHPWFQES RKDPTGPYGD FYVWSDTDEK YQDARIIFVD TEESNWTFDP
     IRRQFFWHRF FSHQPDLNFE NPAVIEALYD VVRFWLDQGI DGFRADAIPY LFEEDGTNCE
     NLPATHTFLQ DLRRMVDSNY PGRVIIAEAN QPPHEVVEYF GTEEAPECHM AFHFPIMPRL
     YYALRDQKAA PIIETLRNTP EIPKGAQWGT FLRNHDELTL EMVPAEERAA MLGWYAPDPR
     MRANIGIRRR LAPLLDNSRS EIELINALLL SLPGSPFLYY GDEIGMGDNI WLDDRDAVRT
     PMQWNPDRNA GFSGADPGKL YLPVIQSLVY NYSMANVEAQ AAHSGSLLRW TRQILSVRKN
     HPVFGLGGFR HIEADHEVVL AYVRELPTGN PEGEDAETIL CVFNLSQHPV AATLDVPEFA
     GRGLRDIFGG QPFPAVGDNG HLTVMLGSHS FYWLRVRSAF SNPSSPFTQA IPVVTSKG
//