ID   D7BH33_ALLS1            Unreviewed;       551 AA.
AC   D7BH33;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
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=Mesil_2014 {ECO:0000313|EMBL:ADH63886.1};
OS   Allomeiothermus silvanus (strain ATCC 700542 / DSM 9946 / NBRC 106475 /
OS   NCIMB 13440 / VI-R2) (Thermus silvanus).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Allomeiothermus.
OX   NCBI_TaxID=526227 {ECO:0000313|EMBL:ADH63886.1, ECO:0000313|Proteomes:UP000001916};
RN   [1] {ECO:0000313|EMBL:ADH63886.1, ECO:0000313|Proteomes:UP000001916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700542 / DSM 9946 / VI-R2
RC   {ECO:0000313|Proteomes:UP000001916};
RX   PubMed=21304690;
RA   Sikorski J., Tindall B.J., Lowry S., Lucas S., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Han C., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Meiothermus silvanus type strain (VI-R2).";
RL   Stand. Genomic Sci. 3:37-46(2010).
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}.
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DR   EMBL; CP002042; ADH63886.1; -; Genomic_DNA.
DR   RefSeq; WP_013158437.1; NC_014212.1.
DR   AlphaFoldDB; D7BH33; -.
DR   STRING; 526227.Mesil_2014; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; msv:Mesil_2014; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_3_0; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001916; Chromosome.
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, ECO:0000313|EMBL:ADH63886.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001916}.
FT   DOMAIN          19..419
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   551 AA;  63849 MW;  277908CE526ABFDF CRC64;
     MAAVSTSDPL WYKDAVFYEL HVRSFQDSNA DGIGDFPGLT SRLDYLQALG VDCLWLMPFY
     PSPLKDDGYD IADYKAINPD YGTLDDFRHF LAEAHARGIR VIADLVVNHT SDQHFWFQEA
     RKGPDNPYYH YYVWSDTPEK YKEARIIFTD TETSNWTFEP AVGKFYWHRF FSSQPDLNYD
     NPKVRQEMLD VVRFWLELGL DGFRVDAVPY LFEREGTNCE NLPETHAFLA ELRRFVDQNF
     PGRLLLAEAN QWPKDVVAYF GTAEQPEFHM CFNFPVMPRI FMALAREEAK PIEEIMRSIP
     EIRPDCQWAI FLRNHDELTL EMVTDEERSF MYAVYAKDPR MKVNVGIRRR LAPLVDGGRR
     QLELLHSILL TLPGSPILYY GDEIGMGDNI YLDDRHGVRT PMQWSIDRNA GFSQADTAKL
     YSPVIVDPPY AYQGVNVEAQ ERSAYSLLQW VRQVIRVRKQ YPVFGRGSLA FLTPNNPKIL
     AYLRSYEGMQ VLVVHNLSRY AQPVALNLSP WKGFTPVEMI GQVAFPPIGE QPYLLTLGPH
     AFFWFRLDQS S
//