ID   I3TS79_TISMK            Unreviewed;      1128 AA.
AC   I3TS79;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   Name=treS {ECO:0000313|EMBL:AFK55617.1};
GN   OrderedLocusNames=TMO_a0214 {ECO:0000313|EMBL:AFK55617.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM1 {ECO:0000313|EMBL:AFK55617.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55617.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55617.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM1 {ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003237; AFK55617.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TS79; -.
DR   KEGG; tmo:TMO_a0214; -.
DR   PATRIC; fig|1110502.3.peg.3868; -.
DR   HOGENOM; CLU_007635_0_1_5; -.
DR   Proteomes; UP000005258; Plasmid pTM1.
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};
KW   Plasmid {ECO:0000313|EMBL:AFK55617.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   DOMAIN          44..438
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1128 AA;  125613 MW;  FC2C2ACF2561F4A6 CRC64;
     MPAPTTPVSS PTVSSPTGAQ GRIIRGADHA PGDPLWYKDA VIYQLHVKSF QDGNDDGIGD
     FPGLISRLDY IAALGVDTIW LLPFYPSPLR DDGYDIADYR DVNRAYGTLG DFKRFLAEAH
     ARGLRVITEL VINHTSDAHP WFQRARRARR GSAQRDFYVW SDDDRKYPET RIIFLDTEKS
     NWTWDPVAGA YYWHRFYSHQ PDLNFDNPRV LDAVLKVMRF WLDMGVDGLR LDAVPYLIER
     EGTNNENLPE THDILKKIRA HLDEHYSDRM LLAEANQWPE DTQEYFGAGD ECHMAFHFPL
     MPRMYMSIAQ EDRFPITDIM RQTPDIPENC QWAIFLRNHD ELTLEMVTET ERTFLWETYA
     SDRRARINLG IRRRLAPLLD RDRRRIELMH SLLLTMPGTP VLYYGDEIGM GDNVHLGDRD
     GVRTPMQWSP DRNGGFSRAD PEQLILPAIM SPLYGHAAVN VETQSRDPHS LLHWTRRMLQ
     VRRRFRAFGR GRLDFLFPGN RRVLAYLRAD DSDTVLCVAN LSRTAQAVEL DLSRFEGRVP
     MELVGGAAFP PIGQLPYLLT LPPYGFYAFA LEPEGRAPVW HLPAPEPLPE HETFVLRRGL
     AQLLEEPHRD RLSKTVLPAW LAMRRWFAGG RDAAATARLD FADPLPGTDG EILLTGVAVA
     RDDGSEDRYA LPLGILWEAD RPDTPALPVR LALARVRQTA RVGLLTDGFA LEGFGRALMR
     ALADGGAEAA PGARLALRPG SAEAVAIAGA LPPGAEVRWM TAEQTNSSVI VGDTAVIKLI
     RRIQPGINPE VEMARHLTGA GYAGVAEFLG ELAWEGPVGE GSAETASLAV IQRFIRNQGD
     GWHWTGDQLA RALDALHHHD HERLEDATAT IRALTRTIGR RLKELHEVLA RPSEDVNFAP
     EIADPATINA WNSRIGQALE TAFDILADHA AAGEDTPLSR AVRRVLTRRR GLAAAVAALA
     EAGTGATLTR IHGDFHLGQL LVSTGDVTLI DFEGEPTRPL ALRRAKDSPW RDVAGLLRSI
     DYVTALPHPA APASDTGAGL EPDDPAHWLL RLRGDMERAF LAGYAGDEAT TTAPDLPALL
     KLFLIEKAAY EVAYEAELRP DWLLLPAAGL ARLAERLVPE TDDVAPDA
//