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Database: UniProt
Entry: A0A1U7NTK9_9DEIO
LinkDB: A0A1U7NTK9_9DEIO
Original site: A0A1U7NTK9_9DEIO 
ID   A0A1U7NTK9_9DEIO        Unreviewed;       552 AA.
AC   A0A1U7NTK9;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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   ORFNames=BOO71_0012370 {ECO:0000313|EMBL:OLV16259.1};
OS   Deinococcus marmoris.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=249408 {ECO:0000313|EMBL:OLV16259.1, ECO:0000313|Proteomes:UP000186607};
RN   [1] {ECO:0000313|EMBL:OLV16259.1, ECO:0000313|Proteomes:UP000186607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOPRI26562 {ECO:0000313|EMBL:OLV16259.1,
RC   ECO:0000313|Proteomes:UP000186607};
RA   Kim J.H., Oh H.-M.;
RT   "Genome Analysis of Deinococcus marmoris KOPRI26562.";
RL   Submitted (JAN-2017) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLV16259.1}.
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DR   EMBL; MSTI01000149; OLV16259.1; -; Genomic_DNA.
DR   RefSeq; WP_075835782.1; NZ_MSTI01000149.1.
DR   AlphaFoldDB; A0A1U7NTK9; -.
DR   STRING; 249408.BOO71_0012370; -.
DR   eggNOG; COG0366; Bacteria.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000186607; Unassembled WGS sequence.
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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          17..417
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   552 AA;  63226 MW;  8B4FA52CEB8C376E CRC64;
     MTQQTPPQWY KSAVFYELSV RTFADGNGDG KGDFPGLTGK LDYLRTLGVD CLWLLPFYPS
     PLRDDGYDVA DYTGIHPDLG TIEDFQFFLA EAHSRGLRVI ADLVTNHTSA EHPWFQAARR
     GPTLPDGSPN EYHDYYVWSD TATEYAGARI IFTDTETSNW TRDEVCGRYY WHRFFSHQPD
     LNFDNPKVIE EILDAGRFWL NTGLDGFRVD AVPYLIERED TNCENLPETH EILKKMRRMV
     DAEYPGRLLL AEANQWPEDV AQYFGTEEDP EFHMCFNFPV MPRLYMSLKK EDTTSIREIM
     GRMPEIPSFG QWATFLRNHD ELTLEMVDDD ERAFMYAAYS PDTRMRINVG IRRRLAPLLN
     NERRRIELLN SVLLALPGSP ILYYGDEIGM GDDLGLADRN GVRTPMQWNA GISGGFSTAW
     PSDCFFPPIS DPVYGYQRVN VQSQERDPGS LLQWTSRQLE ARRQHPAFAH GDLKFVDTDN
     NSVLAFTRSH DNETLLIVCN FGANAQATTL DLSEYVGRTP VTLSGASPFP PVIEGPYTII
     MGRHDYYWLR LN
//
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