ID A0A235GB69_9NOCA Unreviewed; 573 AA.
AC A0A235GB69;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=BDB13_4398 {ECO:0000313|EMBL:OYD70758.1};
OS Rhodococcus sp. OK302.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD70758.1, ECO:0000313|Proteomes:UP000215121};
RN [1] {ECO:0000313|EMBL:OYD70758.1, ECO:0000313|Proteomes:UP000215121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK302 {ECO:0000313|EMBL:OYD70758.1,
RC ECO:0000313|Proteomes:UP000215121};
RA Pelletier D.;
RT "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL Submitted (AUG-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:OYD70758.1}.
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DR EMBL; NPJZ01000001; OYD70758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235GB69; -.
DR OrthoDB; 9800174at2; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000215121; 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 97..442
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 242
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 240..245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 304..308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 374..379
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 375
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 573 AA; 63202 MW; 112FEF33AB605D5A CRC64;
MHTFEVWAPT PESVQVDVDG KVHEMTRAAD GWWRSEIECP NDARYGFVVD GNTLPDPRSP
RQPEGVHQLS QLHALDESVW TDALWTGRQL AGSSVYELHV GTFTPEGTFD AAISRLDHLV
DLGVGFVELM PVNGFNGTHN WGYDGVLWYT VHEGYGGPDG LQRLVNAAHN RGLGVILDVV
YNHLGPSGNY LERFGPYIAD GANTWGRTVN IGGPQSGEVR EYIIRNALRW MRDFHIDGLR
LDAVHALVDH SGTHILEELA VRTETLSAHV GRPLTLIAES DLNDATLITP RAAGGFGLHA
QWDDDIHHAI HTAVSGERQG YYADFGSLES LANTLRRGFF HAGTYSSFRG RAHGRPLDIS
QQAASALLAY TCTHDQIGNR AIGDRPSAYL TPGQLAIKAA LVLLSPYTPM LFMGEEWGAS
TPFQFFTSHP EPELGAATAR GRKAEFAAHG WNTDDIPDPQ DPQTFLRSKL NWDELDAGPH
PRLLSCYRDL LALRKKRIEL TDPWLGHLHV DYDEGKQWIT LRRGALQIVC NLGTDAAHVP
AGGTPILWWD LPTQDETASA TVVPGHSFVV LEN
//
