ID   Q7LYV2_SACSH            Unreviewed;       728 AA.
AC   Q7LYV2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   29-MAY-2024, entry version 19.
DE   SubName: Full=Maltooligosyl trehalose synthase {ECO:0000313|EMBL:AAM81591.1};
GN   Name=treY {ECO:0000313|EMBL:AAM81591.1};
OS   Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC
OS   15437 / B12) (Sulfolobus shibatae).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=523848 {ECO:0000313|EMBL:AAM81591.1};
RN   [1] {ECO:0000313|EMBL:AAM81591.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B12 {ECO:0000313|EMBL:AAM81591.1};
RA   Wu J., Yu W.T., Chen W., Liu L., Wang H., Wang S.X.;
RT   "Cloning and sequence analysis of genes encoding enzymes for trehalose
RT   biosynthesis from thermophilic archaebacterium Sulfolobus shibatae B12.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:5ZCR}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), AND DISULFIDE BONDS.
RX   PubMed=30387780; DOI=10.1107/S2053230X1801453X;
RA   Okazaki N., Blaber M., Kuroki R., Tamada T.;
RT   "Crystal structure of glycosyltrehalose synthase from Sulfolobus shibatae
RT   DSM5389.";
RL   Acta Crystallogr. F Struct. Biol. Commun. 74:741-746(2018).
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DR   EMBL; AY121427; AAM81591.1; -; Genomic_DNA.
DR   PDB; 5ZCR; X-ray; 2.40 A; A/B=1-728.
DR   PDBsum; 5ZCR; -.
DR   AlphaFoldDB; Q7LYV2; -.
DR   SMR; Q7LYV2; -.
DR   GO; GO:0047470; F:(1,4)-alpha-D-glucan 1-alpha-D-glucosylmutase activity; IEA:TreeGrafter.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030980; P:alpha-glucan catabolic process; IEA:TreeGrafter.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd11336; AmyAc_MTSase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 3.
DR   Gene3D; 3.30.1590.10; Maltooligosyl trehalose synthase, domain 2; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012767; Trehalose_TreY.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF216; MALTOOLIGOSYL TREHALOSE SYNTHASE-RELATED; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5ZCR}; Metal-binding {ECO:0007829|PDB:5ZCR}.
FT   DOMAIN          16..407
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         269
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:5ZCR"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:5ZCR"
FT   DISULFID        171..176
FT                   /evidence="ECO:0007829|PDB:5ZCR"
FT   DISULFID        363..382
FT                   /evidence="ECO:0007829|PDB:5ZCR"
SQ   SEQUENCE   728 AA;  86192 MW;  4E2502E37A5F534C CRC64;
     MIIGTYRLQL NKGFTFYDTI EDLDYFKELG VSHLYLSPIL KARPGSTHGY DVVHHSEINE
     ELGGEEGYFK LVKEAKSRGL EIIQDIVPNH MAVHHTNWRL MDLLKSWKNS KYYNYFDHYD
     DDKIILPILE DELDTVIDKG LIKLQKDNIE YRGLVLPIND EGVEFLKRIN CFDNSCLKKE
     DIKKLLLMQY YQLTYWKKGY PNYRRFFAVN DLIAVRIELD EVFRESHEII AKLPVDGLRI
     DHIDGLYNPK EYLDKLRQLV GNDKIIYVEK ILSINEKLRD DWKVDGTTGY DFLNYVNMLL
     VDGSGEEELT KFYENFIGRK INIDELIIQS KKLVANQLFK GDIERLSKLL NVNYDYLVDF
     LACMKKYRTY LPFEDINGIR ECDKEGKLKD EKGIMRLQQY MPAIFAKGYE DTTLFIYNRL
     ISLNEVGSDL RRFSLSIEDF HNFNLSRVNT ISMNTLSTHD TKFSEDVRAR ISVLSEIPKE
     WEERVKYWHD LLRPNIDKND EYRFYQTLVG SYEGFDNKER IKNHIIKVIR EAKVHTTWEN
     PNLEYEKKVL GFIDEVFENS SFRNDFDNFE KKIVYFGYMK SLVATTLKFL SPGVPDIYQG
     TEVWRFLLTD PDNRMAVDFR KLRELLNNLT EKNLELSDPR TKMLYVKKLL QLRREYSLND
     YKPLPFGFQR GKVTVLFSPI VTREVKEKIS IRQKSVDWIR NEEISSGEYN LSELIGEHKV
     VILTEKRE
//