ID B5RAC0_SALG2 Unreviewed; 594 AA.
AC B5RAC0;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 107.
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=SG1567 {ECO:0000313|EMBL:CAR37430.1};
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538 {ECO:0000313|EMBL:CAR37430.1, ECO:0000313|Proteomes:UP000008321};
RN [1] {ECO:0000313|EMBL:CAR37430.1, ECO:0000313|Proteomes:UP000008321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346 {ECO:0000313|Proteomes:UP000008321};
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Sanders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphrey T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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|PIRNR:PIRNR006337}.
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DR EMBL; AM933173; CAR37430.1; -; Genomic_DNA.
DR RefSeq; WP_000095547.1; NC_011274.1.
DR AlphaFoldDB; B5RAC0; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; seg:SG1567; -.
DR HOGENOM; CLU_020726_0_0_6; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000008321; 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:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
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; PTHR43002:SF10; 1,4-ALPHA-GLUCAN BRANCHING ENZYME GLGB; 1.
DR PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 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 Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006337, ECO:0000313|EMBL:CAR37430.1}.
FT DOMAIN 112..453
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 261
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 296
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 594 AA; 65892 MW; 9889364359220D49 CRC64;
MSSKIFCKSW GAEYIAADVV RFRLWATGQQ KVMLRLAGKD QEMQASGDGW FTLDVSGVTP
GTEYNFVLND GMVVPDPASR AQKTDVNGPS YVVDPGSYTW RNTGWKGSRW EQAVVYEMHT
GTFTPEGTFR AAIAKLPYLA ELGVTVIEVM PVAQFGGERG WGYDGVLLYA PHSAYETPDD
FKAFIDAAHG YGLSVVLDIV LNHFGPEGNY LPLLAPAFFH KERMTPWGNG IAYDVDAVRR
YIIEAPLYWL TEYHLDGLRF DAIDQIEDSS ARHVLVEIAQ RIREDITDRP IHLTTEDSRN
IISLHPRDQD GNAPLFTAEW NDDFHNAVHV FATGETQAYY NDFADTPEKH LARALAEGFA
YQGEISPQTG EPRGVKSTGQ PPVAFVDFIQ NHDQVGNRAQ GDRLITLAGA ERTKVLLATL
LLSPHIPLLF MGEEYGESRP FLFFTDFHGD LARAVREGRA KEFADHAGEN VPDPNAPETF
QRSKLNWKQQ HSEEGKAWLA FTRELLLLRQ KHIVPLLSAA RESSGTVLQT APGFIAVSWR
FPGGTLSLAL NISATTVLLP DLPGKTLFAW PNESTGSLSQ HSLIVRLAQG ESAS
//
