ID A0A1B1NEX4_9MICO Unreviewed; 589 AA.
AC A0A1B1NEX4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SGUI_2590 {ECO:0000313|EMBL:ANS79986.1};
OS Serinicoccus hydrothermalis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1758689 {ECO:0000313|EMBL:ANS79986.1, ECO:0000313|Proteomes:UP000092482};
RN [1] {ECO:0000313|EMBL:ANS79986.1, ECO:0000313|Proteomes:UP000092482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT9 {ECO:0000313|EMBL:ANS79986.1,
RC ECO:0000313|Proteomes:UP000092482};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014989; ANS79986.1; -; Genomic_DNA.
DR RefSeq; WP_066641062.1; NZ_CP014989.1.
DR AlphaFoldDB; A0A1B1NEX4; -.
DR STRING; 1758689.SGUI_2590; -.
DR KEGG; serj:SGUI_2590; -.
DR PATRIC; fig|1758689.4.peg.2705; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000092482; 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; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
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; PF02922; CBM_48; 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:UP000092482}.
FT DOMAIN 82..483
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 253
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 290
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 251..256
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 318..322
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 389..394
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 390
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 589 AA; 63765 MW; 7A16E840BAB2ED12 CRC64;
MSETHEFGLW APDAERVDLL LGPRPEDATS VPMEVGEDGW WRAGADPEPH EGRYAFSVDG
GIAIPDPRSR HQPDGVHAPS RLVDTAGFAW SDDAWAGVEL ERAAVYELHV GTFTPEGTFE
AAAGHLDHLV DLGVTVVELM PVAAFPGRHG WGYDGVAPYA VHDPYGGPEG LAAFVDAAHA
AGLAVWLDVV YNHLGPSGNY LSQAGPYFTD RHHTPWGEAV NLDGPGSDEV RDYLLDNTAM
WLEDYHLDGL RLDAVHALHD ERAVHLLEEL AELADQIGER TGIPRSLVAE SDRNDPATVS
RRGPGGAGGL GLHGQWADDV HHALHVLLTG EAQGYYADFA DPAAIPKVLG RTPFFHDGTF
STFRERVHGR PVDLGVTEPW RFVASLQTHD QVGNRAVGDR VHHGIPLGRH AIGAALLLTA
AWTPMLFMGE EWSAGTPWQY FTDHEEEWLA QSIREGRQAE FAEHGWAGQV PDPQDAGTVE
ASTLDWSEPG REPHAQMLEL YRTLLRWRAT TPASARGTTA TVTREADGAG GEVLTVDRPG
VLVLARLGGE GAVRREVPQG THVLISHPPQ EPVDGAVELG PDGVVVMTR
//
