ID   E6VKT6_RHOPX            Unreviewed;      1100 AA.
AC   E6VKT6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
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=Rpdx1_1708 {ECO:0000313|EMBL:ADU43325.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU43325.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) 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; CP002418; ADU43325.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VKT6; -.
DR   STRING; 652103.Rpdx1_1708; -.
DR   KEGG; rpx:Rpdx1_1708; -.
DR   eggNOG; COG0366; Bacteria.
DR   eggNOG; COG3281; Bacteria.
DR   HOGENOM; CLU_007635_1_2_5; -.
DR   OrthoDB; 9805159at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS08380-MONOMER; -.
DR   Proteomes; UP000001402; 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; 3.90.1200.10; -; 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          30..429
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   1100 AA;  125282 MW;  607FFC26FE5D06A3 CRC64;
     MNEMSPIVAN DRPGDDASDE LWYKDAIIYQ LHVKAFADSN NDGIGDFAGL TEKLDYLQEL
     GVNTLWLLPF YPSPQRDDGY DIADYGSINP DFGTMKDFRR FIFEAKRRNL RVITELVVNH
     TSDQHAWFKR ARRSPKNSSA RNWYVWSDTD QKYQGTRIIF TDTEKSNWTW DPEAGQYYWH
     RFFSHQPDLN FDNPRVVGAV VKVMKRWLDN GVDGFRLDAI PYLCERDGTN NENLPETHAV
     IKRLRAELDA YAKGKLLLAE ANQWPEDVQQ YFGDSDECHM AYHFPLMPRI YMAIAQEDRF
     PITDIMRQTP EIPPNCQWAM FLRNHDELTL EMVTDVERDY LWKTYAADPR ARINVGIRRR
     LAPLMDNDRR KIELMNSLLL SFPGTPIIYY GDEIGMGDNI YLGDRNGVRT PMQWSSDRNG
     GFSRADPARL YAPPIMDPVY GYASVNVEAQ QRSLSSLLSA MKRLIAVRKS TSAFGRGSMT
     FIRPSNRAVL AYVRQHEDEV ILCVANLSRA AQATELDLSP WKERVPQEML GRTKFPPIGE
     LPYMITLAPF GFYWFKLEEP GTAAHVAPVS TVPEFVTLVV PLGSTWMTLG RTRSMFEHEV
     LPTFLSRTRW FPERNPRAIH PRLTSAIPFA NDGDNRPWLA LFEATLRGTT ARYLLPMQID
     WVRFDRERYN PRAYAAVRQG AREGTLLDVA ADPSFVDLLL QNVRSALTVI GDDGNRLEFR
     PGSLLAERPA GPFENIRPVD AEQSNSTSLI DEDYVVKLYR RLQVGINPEL EMGRFLTEVA
     GYRNTPALLG SVELVEGDTT TAIAVVHEFI GNQGDGWTLT AGYLDRYVDE QRVLTGNPEA
     AESDQFAPYL HFMQHTGRRV AEMHIALAGH PELPDFAPEP IGPDEARSWV ATVSAAAERV
     LGELRRRRDG FSDPDKALVD RLLAAREILM GRIGEFLGDD GGLNIRHHGD FHLGQMLIVK
     DDIYIIDFEG EPRRTLAERR AKAPAARDVA GLVRSIDYST TAALTRALKT PPDEPGRLNE
     ALELWRIRAT TAFLDGYRQT MGESPVWPAD PDAADRWLDF FLIEKALYEI DYEIAHRPDW
     LRVPLAGILR ILSPPPEEFP
//