ID K9W3E3_9CYAN Unreviewed; 615 AA.
AC K9W3E3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=Cri9333_4076 {ECO:0000313|EMBL:AFZ14878.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ14878.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ14878.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ14878.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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; CP003620; AFZ14878.1; -; Genomic_DNA.
DR AlphaFoldDB; K9W3E3; -.
DR STRING; 1173022.Cri9333_4076; -.
DR KEGG; cep:Cri9333_4076; -.
DR PATRIC; fig|1173022.3.peg.4400; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_020726_2_0_3; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000010472; 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:0016757; F:glycosyltransferase activity; 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; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR022567; DUF3459.
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; 2.
DR Pfam; PF02922; CBM_48; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006337};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 122..466
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 268
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT ACT_SITE 305
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-1"
FT BINDING 266..271
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 330..334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT BINDING 398..403
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-2"
FT SITE 399
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR006337-3"
SQ SEQUENCE 615 AA; 69954 MW; A7F295BC7D3023C8 CRC64;
MAQGQALLNM KIGSNYLGDN RCEFIVWAPE LKEVAVKITA PQERLLPMQK DEAGYWKVTA
EGISPGTHYF YKLEGDAERP DPASHFQPEG VHGASQVIDH STIQWSDDQW SGVPLDEMII
YELHVGTFTP EGSFDAIIPR LRELYEFGVN AIEIMPVAQF PGDRNWGYDG TYPFAVQNSY
GGVEGLKRLV DACHQQGIAV IMDVVYNHFG PEGNYISNYG PYFTATYKTP WGMAVNFDDK
RSDGVRNYFI ENALYWFENC HIDALRLDAI HAIYDLGAKH FLEELSERVE TLSQQVGRKL
YLIAESDLND VRVIRDRTLG GHSMDAQWSD DFHHALHTIL TGETIGYYKD FGKCEQLATA
LKESFVYSWK LSANRERYHG NDAKDFPGQQ FVIATQNHDQ VGNRMLGERL SNLVSFDALK
LAAAALLLSP NVPMLFMGEE YGEESPFLYF VSHSDHDLVE AVRKGRKEEF KDFHIEGEFQ
DPFSQETFDQ CILKWEKRQE GKNKALLELH QHLIQLRRTI PALKSLDKQN LEISCSEADK
LIQMRRGNQE SEIFCVMNFS KQDVTFKPDV ADSSWSKILD SADEKWFGAG AKLPEQLNSG
QEFTIPPLSF ALFGK
//
