(data stored in ACNUC7421 zone)

SWISSPROT: C4KE20_SULIK

ID   C4KE20_SULIK            Unreviewed;       561 AA.
AC   C4KE20;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 56.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
GN   OrderedLocusNames=M164_0512 {ECO:0000313|EMBL:ACR41143.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR41143.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR41143.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-alpha-D-glucosidic
CC       linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to
CC       yield trehalose and (1->4)-alpha-D-glucan.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; CP001402; ACR41143.1; -; Genomic_DNA.
DR   RefSeq; WP_012735546.1; NC_012726.1.
DR   ProteinModelPortal; C4KE20; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ACR41143; ACR41143; M164_0512.
DR   KEGG; sid:M164_0512; -.
DR   HOGENOM; HOG000155669; -.
DR   KO; K01236; -.
DR   OMA; FTPMLFM; -.
DR   OrthoDB; POG093Z00WH; -.
DR   BioCyc; SISL426118:GI01-523-MONOMER; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001479; 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   Gene3D; 2.60.40.10; -; 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; IPR015156; Maltooligo_trehalose_arc_C.
DR   InterPro; IPR012768; Trehalose_TreZ.
DR   Pfam; PF09071; Alpha-amyl_C; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF02922; CBM_48; 1.
DR   PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02402; trehalose_TreZ; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KE20.
DR   SWISS-2DPAGE; C4KE20.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:ACR41143.1}.
FT   DOMAIN      109    487       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    255    255       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    286    286       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        380    380       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   561 AA;  64290 MW;  B6060C996948FD1B CRC64;
     MAFGYRLDRN GVTFNLWAPY QRNVKLKILN KGIYEMERDE KGYFTITLNN VKVGDRYKYI
     LDDGSEVPDP ASRYQPEGVH GHSEIISLDF KGDDETGVKV KREDLIIYEL HTSTFTSEGT
     FEGVIKKLDY LKELGVTAIE IMPIAQFPGK KDWGYDGVYL YAVQNSYGGP IGFRNLVNEA
     HKLGLAIILD VVYNHVGPEG SYMAKLGPYF SEKYKTPWGL AFNFDDAGSD EVRKFILENV
     EYWINEFHVD GFRLDAVHAI IDNSPKHILE DIADVVHKYG KIVITESDLN DPRVVNPKEK
     CGYNTDAQWV DDFHHAIHAF LTGERQGYYS DFGSLDDIVK SYKEVFVYDG KYSNFRRKTH
     GKPVGDLDGC KFVVYIQNHD QVGNRGGGER LIKLVDKESY KIAAALYMLS PYIPMIFMGE
     EYGEENPFYY FSDFSDPKLI QGVREGRKRD NGQETDPQSD STFNSSKLSW KVNDDIFSFY
     KTLIKIRKEY GLACNRKLTV ENGNHWLTVK GNGYLVVYVF SQSIIEMKYR GTLVLSSNNS
     FPSQIVENKY KLEKGFALYK L
//

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