ID   A0A158DPA7_9BURK        Unreviewed;      1132 AA.
AC   A0A158DPA7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=AWB77_05568 {ECO:0000313|EMBL:SAK96036.1};
OS   Caballeronia fortuita.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777138 {ECO:0000313|EMBL:SAK96036.1, ECO:0000313|Proteomes:UP000054903};
RN   [1] {ECO:0000313|Proteomes:UP000054903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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}.
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DR   EMBL; FCNX02000017; SAK96036.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158DPA7; -.
DR   STRING; 1777138.AWB77_05568; -.
DR   Proteomes; UP000054903; 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; 3.90.1200.10; -; 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; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   InterPro; IPR012811; TreS_maltokin_C_dom.
DR   NCBIfam; TIGR02457; TreS_Cterm; 1.
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.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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          28..422
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1102..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1132 AA;  128175 MW;  F7CDCE61952B0BEB CRC64;
     MDTRVKRNKK ASILSDDPLW YKDAIIYQVH IKSFFDANND GIGDFPGLLA KLDYIAELGV
     DAIWLLPFYP SPRRDDGYDI ADYRNVHPDY GTIADVKRFI QEAHARGIRV ITELVINHTS
     DQHPWFQRAR HAKPGSNHRN YYVWSDTDKK YEETRIIFID TEPSNWTHDP VAGQYYWHRF
     YAHQPDLNFD NPAVIKEVLS VMRFWLDMGI DGLRLDAVPY LVEREGTNNE NLPETHEILK
     KIRATIDAEY PNRMLLAEAN QWPEDVKEYF GDEDECHMAF HFPLMPRIYM SIASEDRFPI
     TDIMRQTPDL AETNQWAIFL RNHDELTLEM VTDSERDYLW NTYASDRRAR LNLGIRRRLA
     PLMERDRRRI ELINSLLLSM PGTPVIYYGD ELGMGDNIHL GDRDGVRTPM QWSSDRNGGF
     SRADPEQLVL PPVMGSLYGY DAVNVESQSR DPHSLLNWTR KMLAVRRSKH AFGRGTIRFL
     RPANRKILAY LRELEGEPPI LCVANLSRAP QAVELDLSEF DGSVPLEMTA DSPFPAIGKL
     TYLLTFPPYG FLWFQLCPGN MRPAWAQAPS EQLPEFVTMV IRAGQTGPTP ENVRLLESEV
     LPNYLSKRRW FASKDQKLHA VRLAALTTIE GAGFAFTEIE ADVGDHCERY VLPLSIAWGT
     ETTSPLYMQL ALARVRRNRN IGHLTDAFAV PQFTYGVMRK LKERAVVPTV QKSEIRFLPT
     ERLDELNYYP ADPPEIRWLA AEQSNSSLVI GEKVVLKLVR RVVGGIHPEA EMSRYLTKLG
     YANTGPLYGE VVRVDPQGVP HTLIILQGFI DNQGDAWNYA LDYLRRTVDE LAVVVESDEH
     TQERDAQAEG FAGYASIAGI IGKRLGELHV ALASPTDDEA FAPQRATAED VKGWVDGTLK
     LLESALDILA QKIGDFSEHD RFLAQSLLDR RDMLVDTVKK LVASDADALC IRIHGDFHLG
     QVLMAQGDAY LIDFEGEPAR ALDERRKKTS PLRDVAGLLR SLSYASAAAQ STTENAPAQT
     ADRKRALFER LRASAEESFL RQYTEAIAAS PETIAAEDVF QPLLDLFLIE KAAYEIRYEA
     ANRPTWIGLP LRGLASLASR LLGDTGEPPA PGTRPVIGAT KDNPDGTHHE HS
//