ID R7WW49_9NOCA Unreviewed; 611 AA.
AC R7WW49;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=Rrhod_0187 {ECO:0000313|EMBL:EOM78359.1};
OS Rhodococcus rhodnii LMG 5362.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1273125 {ECO:0000313|EMBL:EOM78359.1, ECO:0000313|Proteomes:UP000013525};
RN [1] {ECO:0000313|EMBL:EOM78359.1, ECO:0000313|Proteomes:UP000013525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 5362 {ECO:0000313|EMBL:EOM78359.1,
RC ECO:0000313|Proteomes:UP000013525};
RX PubMed=23788540;
RA Pachebat J.A., van Keulen G., Whitten M.M., Girdwood S., Del Sol R.,
RA Dyson P.J., Facey P.D.;
RT "Draft Genome Sequence of Rhodococcus rhodnii Strain LMG5362, a Symbiont of
RT Rhodnius prolixus (Hemiptera, Reduviidae, Triatominae), the Principle
RT Vector of Trypanosoma cruzi.";
RL Genome Announc. 1:e00329-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOM78359.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APMY01000004; EOM78359.1; -; Genomic_DNA.
DR RefSeq; WP_010836266.1; NZ_APMY01000004.1.
DR AlphaFoldDB; R7WW49; -.
DR STRING; 38312.GCA_000720375_11124; -.
DR PATRIC; fig|1273125.3.peg.186; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000013525; 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; 3.20.20.80; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000013525}.
FT DOMAIN 51..452
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 611 AA; 69782 MW; 59313DD73ABC84A5 CRC64;
MGHEQARSAE GTPQADTDAE GHVIEAQADD FAHARELPED TEWFKTAVFY EVLVRAFYDS
TGDGVGDLRG LTSKLDYLDW LGVDCLWLPP FYDSPLRDGG YDIRDFRKVL PDFGTVDDFV
ELFDEAHKRG IRVITDLVMN HTSDTHAWFQ ASRSDPDGPY GDFYVWADDD TGYPDARIIF
VDTETSNWTW DPVRGQYYWH RFFSHQPDLN YDNPEVQEAM LAVLRFWLDL GIDGFRLDAV
PYLFEREGTN CENLPQTHAF LKKCRAVIDA EYTGRVLLAE ANQWPSDVVE YFGEPDVGDE
CHMAFHFPLM PRIFMAVRRQ NRFPISEILA QTPPIPQSAQ WGIFLRNHDE LTLEMVSDEE
RDYMYAEYAQ DPRMKANIGI RRRLAPLLEN DRNQLELFTA LLLSLPGSPV LYYGDEIGMG
DNIWLGDRDS VRTPMQWTPD RNAGFSRADP GRMYLPVIMD PTYGYQSVNV EAQMNSTNTL
LHWTRRMIEV RKQHPAFGKA SFTEIGSLNP AVLSYLREMP LGPDGEYSDV ILCVNNLSRY
PQAVQLDLTA FAGRIPVELT GSVPFPTICD GEYQITLPGH GFYWFSLQPD PATSDAAPHR
HVSSEAEEAV R
//
