ID   Q2JDB8_FRACC            Unreviewed;       593 AA.
AC   Q2JDB8;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   02-SEP-2026, entry version 130.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938, ECO:0000256|NCBIfam:TIGR02402};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268, ECO:0000256|NCBIfam:TIGR02402};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00033284, ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00032057, ECO:0000256|PIRNR:PIRNR006337};
GN   OrderedLocusNames=Francci3_1347 {ECO:0000313|EMBL:ABD10724.1};
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Frankiales;
OC   Frankiaceae; Frankia.
OX   NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD10724.1, ECO:0000313|Proteomes:UP000001937};
RN   [1] {ECO:0000313|EMBL:ABD10724.1, ECO:0000313|Proteomes:UP000001937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3
RC   {ECO:0000313|Proteomes:UP000001937};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC         [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC         alpha-D-glucan.; EC=3.2.1.141;
CC         Evidence={ECO:0000256|ARBA:ARBA00034013,
CC         ECO:0000256|PIRNR:PIRNR006337};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005199, ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRSR:PIRSR006337-1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|PIRNR:PIRNR006337}.
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DR   EMBL; CP000249; ABD10724.1; -; Genomic_DNA.
DR   RefSeq; WP_011435790.1; NC_007777.1.
DR   AlphaFoldDB; Q2JDB8; -.
DR   STRING; 106370.Francci3_1347; -.
DR   KEGG; fra:Francci3_1347; -.
DR   eggNOG; COG0296; Bacteria.
DR   HOGENOM; CLU_020726_2_0_11; -.
DR   OrthoDB; 9800174at2; -.
DR   PhylomeDB; Q2JDB8; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001937; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11325; AmyAc_GTHase; 1.
DR   CDD; cd02853; E_set_MTHase_like_N; 1.
DR   Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012768; Trehalose_TreZ.
DR   InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR   NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR   PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR   PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF11941; DUF3459; 1.
DR   PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001937}.
FT   DOMAIN          106..473
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          460..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   ACT_SITE        289
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT   BINDING         250..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         314..318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   BINDING         383..388
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT   SITE            384
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ   SEQUENCE   593 AA;  64651 MW;  2750DBB49AC7922B CRC64;
     MSTLRLWAPE AKTVSLVVAG SAGDSTHEMT AGKRGWWWVN VPSAKHGTDY AFLLDDGSEE
     LPDPRSAWQP GPLGVHGRSR LVDHSTFPWT DGTWRGIALA GSVLYELHVG TFTPEGTFDA
     AIGKLDHLVE LGIDAIELLP VNAFPGRHGW GYDGVGLFAV HEPYGGPDGL KRFVDAAHAR
     GLGVIMDVVY NHLGPDGNYL GRFGPYFTDR YSTPWGPAVN LDAPGSDEVR TFIIDSALSW
     LRDYHCDGLR LDAVHAFQDS RALHLLEEIA EAVHRLGAQL RRPLFAVAES DLNDPKLVAA
     PEAGGYGLDG QWCDDIHHAL WATLSGERQG YYGDFGSIST LAHALTSGFV HDGGYSTFRG
     RSHGRPIPPT TPAYRFVTFL QNHDQIGNRA AGDRASATLS DGLLRIGAAL LLTSAVTPML
     FMGEEWGART PWQYFTDHTA PGLGDAVREG RRAEFAAHGW EPQDVPDPQD PATFQQSKLD
     WSEPGREGHS DLLDWHRRLI ALRRRLPALT DPAWSSVACT FDEEARWLVV RRGDVAIVVN
     LAAERQAVPL DGVPFDAPAA SAHGFTYMPG RVELDGESVV IIRLLPPVEP TAG
//