ID A0A2A4KDV8_9ACTN Unreviewed; 568 AA.
AC A0A2A4KDV8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PCG81852.1};
GN ORFNames=CIB93_33220 {ECO:0000313|EMBL:PCG81852.1};
OS Streptomyces sp. WZ.A104.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2023771 {ECO:0000313|EMBL:PCG81852.1, ECO:0000313|Proteomes:UP000217525};
RN [1] {ECO:0000313|EMBL:PCG81852.1, ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|EMBL:PCG81852.1,
RC ECO:0000313|Proteomes:UP000217525};
RA Xu L., He S., Yan X.;
RT "Isolation and Genomic Analysis of a Bioactive Actinomycete Associated with
RT Cyanobacterium Lyngbya cf. aestuarii.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000217525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WZ.A104 {ECO:0000313|Proteomes:UP000217525};
RA Jiao Y., Han B.;
RL Submitted (SEP-2017) 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:PCG81852.1}.
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DR EMBL; NWVL01000096; PCG81852.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4KDV8; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000217525; 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 Reference proteome {ECO:0000313|Proteomes:UP000217525};
KW Transferase {ECO:0000313|EMBL:PCG81852.1}.
FT DOMAIN 31..433
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 568 AA; 65860 MW; 582A9DA8C9D1751D CRC64;
MIVNEPVHDT FEDTPAKDRD PDWFKRAVFY EVLVRSFQDS NGDGIGDLKG ITAKLDYLQW
LGVDCLWLPP FFKSPLRDGG YDVSDYTAVL PEFGDLADFV EFVDASHQRG MRVIIDFVMN
HTSDQHEWFQ QSRTDPDGPY GDYYVWADDD KQFQDARIIF VDTETSNWTF DPVRKQYYWH
RFFSHQPDLN YENPAVQEEI LAALRFWLDL GIDGFRVDAV PYLYQREGTN CENLPETHNF
LKRVRKEIDA NYPDTVLLAE ANQWPEDVVD YFGDYEAGGD ECHMAFHFPV MPRIFMAVRR
ESRYPVSEIL AKTPAIPKNC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
IRRRLAPLLD NDRNQIELFT ALLLSLPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
DRNAGFSSSD PGRLYLPTIM DPVYGYQVTN VEASMASPSS LLHWTRRMIE IRKQNPAFGL
GEYTELPSSN PAVLAFTREY KDDLVLCVHN FSRFAQPTEL DLRSFNGRHP VELIGGVRFP
AIGQWPYLLT LAGHGFYWFR LRKDAPPA
//
