GenomeNet

Database: UniProt
Entry: Q47SE5_THEFY
LinkDB: Q47SE5_THEFY
Original site: Q47SE5_THEFY 
ID   Q47SE5_THEFY            Unreviewed;       606 AA.
AC   Q47SE5;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN   OrderedLocusNames=Tfu_0584 {ECO:0000313|EMBL:AAZ54622.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54622.1};
RN   [1] {ECO:0000313|EMBL:AAZ54622.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54622.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000088; AAZ54622.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47SE5; -.
DR   STRING; 269800.Tfu_0584; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; tfu:Tfu_0584; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   OrthoDB; 3203135at2; -.
DR   BRENDA; 5.4.99.16; 6298.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000313|EMBL:AAZ54622.1};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAZ54622.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          39..441
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  70201 MW;  B4E258656FAC7C88 CRC64;
     MTTQPAPGAR PTPTGSVPDT FTHAKPRDPY WYKHAVFYEV LVRGFYDSNG DGTGDLRGLI
     EKLDYLQWLG IDCLWLLPIY ESPLRDGGYD VSDYMKILPE FGRISDFVEL VEKAHQRGIR
     VITDLVMNHT SDQHPWFQAS RHDPDGPYGN FYVWSDTTER YSDARIIFID TEQSNWTYDE
     VRGQYYWHRF FSHQPDLNFE NPDVQDAILE VMRFWLDLGI DGFRLDAVPY LYEREGTNCE
     NLKETHEFLK RIRAEVDRLY PDRVLLSEAN QWPADVVDYF GDYESGGDEC HMNFHFPLMP
     RMFMAVRREQ RYPISEILAQ TPPIPRNCQW AIFLRNHDEL TLEMVSDEER DYMYSEYAKD
     PRMRANMGIR RRLAPLLEND LNQIKLFTAL LLSLPGSPVL YYGDEIGMGD NIWLGDRDSV
     RTPMQWTPDR NAGFSRCDPG RLYLPVIMDP IYGYQAINVE AQQNNPNSLL NWTRNMIQIR
     KQHPVFGTGD FTELHASNPS VFAFVREYGD DRMLCVNNLS RFPQPVELDL RRFEGITPIE
     CTGGVHFPPI GELPYLLTLP GHGFYWFQLP PVAEEQPLAQ PVTTVPAAPQ PPAPADRPAS
     DPTQRS
//
DBGET integrated database retrieval system