ID A0A2S5W4B3_9MICO Unreviewed; 572 AA.
AC A0A2S5W4B3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:PPF85533.1};
GN ORFNames=C5B96_05505 {ECO:0000313|EMBL:PPF85533.1};
OS Subtercola sp. Z020.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Subtercola.
OX NCBI_TaxID=2080582 {ECO:0000313|EMBL:PPF85533.1, ECO:0000313|Proteomes:UP000238959};
RN [1] {ECO:0000313|EMBL:PPF85533.1, ECO:0000313|Proteomes:UP000238959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z020 {ECO:0000313|EMBL:PPF85533.1,
RC ECO:0000313|Proteomes:UP000238959};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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}.
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:PPF85533.1}.
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DR EMBL; PSTT01000042; PPF85533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5W4B3; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000238959; 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:0016740; F:transferase activity; 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 Transferase {ECO:0000313|EMBL:PPF85533.1}.
FT DOMAIN 26..426
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 572 AA; 65518 MW; 198429E539CAF12C CRC64;
MSFTAPIQLP GLTLDPQWYR RSVFYEVMIR SFVDGNGDGS GDLAGLVSKL DYLQWLGIDG
LWLPPFFDSP LRDGGYDISD YRSILPEFGS IDEFRDLVTK AHERNMRVVI DLPLNHTSDQ
HEWFQQSRSD PEGPYGDFYV WSDTDTKYEN VRIIFVDTEE SNWTFDPVRR QFFWHRFFSH
QPDLNFENPA VHEAMFEIVR FWLDLGVDGF RLDAIPYLYV SEEGNGEGEP KTHEFVAKLR
QMVDREYPGR IMIAEANQWP REVAAFFGTE EEPECHMAFD FPVMPRIFYS LRSQTATELI
RVLSDVTAIP EGAGWGVFLR NHDELTLEMV SEEYRQAMYG WYAYDPRMRA NIGIRRRLAP
LLDNSRAELE LAHALLFSLS GSPFLYYGDE IGMGDNIWLP DRDSSRTPMQ WTPDRNAGFS
TADPGKLFLP VVQSLVYNYT VVNVESQLAQ SRSMLHWVRN VIHVRKAHPA FGLGSLDIVP
TSHDSILSFV RSYAGSDSQW GDAPERILCV FSFAHNPVSV TLQLPEFAGR RLSDLFGGGE
FPTIGDDGTL TLTLATQSFY WLRIGQAGVE VY
//
