ID   A0LSP1_ACIC1            Unreviewed;       556 AA.
AC   A0LSP1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=Acel_0678 {ECO:0000313|EMBL:ABK52451.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52451.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK52451.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
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; CP000481; ABK52451.1; -; Genomic_DNA.
DR   RefSeq; WP_011719514.1; NC_008578.1.
DR   AlphaFoldDB; A0LSP1; -.
DR   STRING; 351607.Acel_0678; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ace:Acel_0678; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   InParanoid; A0LSP1; -.
DR   OrthoDB; 3203135at2; -.
DR   Proteomes; UP000008221; 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:ABK52451.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT   DOMAIN          26..424
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   556 AA;  64731 MW;  78AC8D8BBE65FBB5 CRC64;
     MSALPHEPAP IPPVDPLWYK RAVFYEVLVR GFYDSNNDGT GDLRGLIAKL DYLQWLGVDC
     IWLLPIYASP MRDGGYDISD YFSILPEYGD LGDFVQLVDE THRRGMRIIA DLVMNHTSDQ
     HPWFQASRID PDGPYGDFYV WSDTDTKYKD ARIIFVDTEK SNWTFDPVRG QYYWHRFFSH
     QPDLNYENPA VQEAMLAVLR FWLDLGIDGF RLDAVPYLFE EEGTNCENLP KTHEYLKRIR
     KEVDQLYPDK VLLAEANQWP ADVVQYFGDG DECHMAFHFP LMPRIFMAVR REQRFPISEI
     LAQTPRIPEN CQWGIFLRNH DELTLEMVTD EERDYMYREY AQDPRMKANI GIRRRLAPLL
     DNSRDQMELF TALLLSLPGS PVMYYGDEIG MGDNIWLGDR DSVRTPMQWT PDRNAGFSQC
     DPGRLYLPVI MDAVYGYQAL NVEAQMRSPH SLLHWVRRMI DIRKRHPTFG CGSYEELGAS
     NPSILAFVRE FGDDRVLCVN NLSRFPQPVE LDLRRYEGVV PIEMTGGVPF PRIGELPYLL
     TLPGHGFYWF MLPTHP
//