ID E8NFS8_MICTS Unreviewed; 583 AA.
AC E8NFS8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|ARBA:ARBA00015938, ECO:0000256|PIRNR:PIRNR006337};
DE Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE EC=3.2.1.141 {ECO:0000256|ARBA:ARBA00012268, ECO:0000256|PIRNR:PIRNR006337};
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=MTES_1009 {ECO:0000313|EMBL:BAJ73973.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ73973.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ73973.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ73973.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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; AP012052; BAJ73973.1; -; Genomic_DNA.
DR RefSeq; WP_013584100.1; NC_015125.1.
DR AlphaFoldDB; E8NFS8; -.
DR STRING; 979556.MTES_1009; -.
DR KEGG; mts:MTES_1009; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_020726_2_0_11; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000008975; 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-UniPathway.
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; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; 2.
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}.
FT DOMAIN 105..447
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 246..251
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 310..314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 379..384
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 380
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 583 AA; 63786 MW; 1BFCFB48A7B1A647 CRC64;
MSIDVWAPRA ERVRLRRLDD SGDSVVEDIE MVGAADGWWT APVELADGER YGFVLGDGDD
LRPDPRSRRQ PGGVHEASAW FDPSVYAWND AAWTGKQLAG GLIYELHLGT FTPEGTLDAA
IGRLEHLVDL GVTHVELLPV NGFNGTWNWG YDGVLWYTVH EAYGGPEAYQ RFVDAAHAAG
LAVIQDVVYN HLGPSGNYLP LFGEYLREGS RNTWGDSVNL DEDAVRAYIV ENALMWMSDY
HVDGLRLDAV HALLDHRDPH VLQEIAERTD ALSAHRGIPL TTIAESDMND PKLILPREAG
GYGLTAQWSD DWHHTAHVAL TGETIGYYED FADLDAFRKV SEGGFFHDGT YSSFREEKHG
KPIPAAVPNW RLVTFAQDHD QIGNRAAGDR LSQTLGYERL AAAAVLTLTA PGTPMLFMGE
EWGATTPWQF FTSHPEPELG KATAEGRIAE FAKMGWDEST VPDPQDPSTF ENSKLDWDEV
GEGDHAQLLG LYRELAKLRR ERPELTDPSR EGLSAAAREA TGGRVYELRR GDLVVVVNLS
DAEASASVVP GARVLLATVE GVVLEGTELT VPAGGSAIAG PAL
//
