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Database: UniProt
Entry: A0A3S3E5M1_9NOCA
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ID   A0A3S3E5M1_9NOCA        Unreviewed;       585 AA.
AC   A0A3S3E5M1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
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   Name=treZ {ECO:0000313|EMBL:RVW05899.1};
GN   ORFNames=EGT50_03765 {ECO:0000313|EMBL:RVW05899.1};
OS   Rhodococcus xishaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=2487364 {ECO:0000313|EMBL:RVW05899.1, ECO:0000313|Proteomes:UP000283479};
RN   [1] {ECO:0000313|EMBL:RVW05899.1, ECO:0000313|Proteomes:UP000283479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51113 {ECO:0000313|EMBL:RVW05899.1,
RC   ECO:0000313|Proteomes:UP000283479};
RA   Li L., Lin H.W.;
RT   "Rhodococcus spongicola sp. nov. and Rhodococcus xishaensis sp. nov. from
RT   marine sponges.";
RL   Submitted (NOV-2018) 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:RVW05899.1}.
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DR   EMBL; RKLO01000001; RVW05899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S3E5M1; -.
DR   OrthoDB; 9800174at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000283479; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283479}.
FT   DOMAIN          99..444
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          54..74
FT                   /note="Disordered"
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   585 AA;  65511 MW;  67AD74091B2EDEAC CRC64;
     MHTFEVWAPI PQSVRVHVDG TEHDMSRSPD GWWHADVDAE SGARYGFVLD DSPTVLPDPR
     SPRQPDGVHL PSQLHDLDPA GWTDTMWTGR QLAGSVVYEL HVGTFTQDGT FDAAIEKLDH
     LVELGVGFVE LMPVAAFNGA HNWGYDGVLW YAVHEEYGGP DGLQRFVDAC HGRGLAVVLD
     VVYNHLGPSG NYLDRFGPYL ADGANSWGRV INLSDKDSGE VRRFIIENAL RWFREFHIDA
     LRLDAVHALV DNSTTHLLEE LSIEVHSLAT HLRRPLTLIA ESDLNDPKII TARAAGGYGL
     SAQWDDDVHH AIHAAVSSER QGYYGDFGSL QALAHTLTHG YFHGGTYSTF RGRNHGRPMD
     IRRIPADTML AYTCTHDQVG NRATGDRPSE YLTPGQLAVK AALVLCSPYT PMLFMGEEWG
     ARTPFQYFTS HPEPELGEAT AQGRRREFAE HGWDTDDIPD PQDPATFLRS KLDWTEPQQP
     AHARLLDCYR RLITLRHSRA DLTDPWLEHL KVEYDEDKRW IALIRGDLRI VFNLGPSRVT
     VPVGGVPLLW WEEPEVDETA SAITLPGHSF AVLDAEPIRV CTSRR
//
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