ID A0A0M2ZCN6_9MYCO Unreviewed; 574 AA.
AC A0A0M2ZCN6; A0A1A0QW66;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 ORFNames=BST23_23560 {ECO:0000313|EMBL:ORA60131.1};
OS Mycolicibacterium elephantis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA60131.1, ECO:0000313|Proteomes:UP000192772};
RN [1] {ECO:0000313|EMBL:ORA60131.1, ECO:0000313|Proteomes:UP000192772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FI-09383 {ECO:0000313|EMBL:ORA60131.1,
RC ECO:0000313|Proteomes:UP000192772};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORA60131.1}.
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DR EMBL; MVHP01000039; ORA60131.1; -; Genomic_DNA.
DR RefSeq; WP_046753552.1; NZ_MVHP01000039.1.
DR AlphaFoldDB; A0A0M2ZCN6; -.
DR STRING; 81858.BST23_23560; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000192772; Unassembled WGS sequence.
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; 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}.
FT DOMAIN 79..444
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 53..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 281
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 242..247
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 306..310
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 376..381
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 377
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 574 AA; 64241 MW; 7B2D7672FE6075CC CRC64;
MTQFAVWAPT PERVRLDVDG TRYDMDRSED GWWRAEVSAR SDARYGFVLD DDETVLPDPR
SPRQPDGVHD RSQLWSPDPD AWTDGNWAGR SIEGTVIYEL HVGTFTPQGT FDAAIEKLDY
LVDLGVDFVE LMPVNAFGGT HGWGYDGVLW YAVHEPYGGP DGLVRLIDAC HRRGLGVLID
AVFNHLGPSG NYLPRFGPYL SSGSNPWGES INISGPDADE VRRYILDCAL RWMRDFHADG
LRLDAVHALV DTTAIHILEE LSAETDALAE ELGRPLSLIA ESDLNDPRLI TPRDRGGYGM
TAQWDDDIHH AIHAAVSGER QGYYGDFGSL EALATTLKNG YFHAGTYSSF RHRRHGRPLD
TSSIPGTRLL AYTLTHDQVG NRAVGDRPSQ NLTFGQLAVK AALVLTSPYT AMMFMGEEWG
SSSPFQFFSS HPEPELARAT AEGRKHEFAE HGWDADEIPD PQDPETFLRS KLRWDEVDDG
EHGRLHRIYQ QLIAVRNDHP EFTDPWLDHL RIEYDEAQRW LVIHRGAFAV ACNLGAEPVD
VPVTGELVLA WDEPTIGAKS TRLPAHSFVI VRRD
//
