ID A0A0Q5L8U0_9MICO Unreviewed; 579 AA.
AC A0A0Q5L8U0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ASF82_06455 {ECO:0000313|EMBL:KQR47005.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR47005.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR47005.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47005.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR47005.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR47005.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR47005.1}.
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DR EMBL; LMOX01000001; KQR47005.1; -; Genomic_DNA.
DR RefSeq; WP_056054884.1; NZ_LMOX01000001.1.
DR AlphaFoldDB; A0A0Q5L8U0; -.
DR STRING; 1736282.ASF82_06455; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000051005; 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:UP000051005}.
FT DOMAIN 26..426
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 579 AA; 66137 MW; E0BD2492C2079129 CRC64;
MSFTAPIQQP GLTLDPQWHR RAVFYEVMVR SFVDSNGDGA GDLQGLLSRL DYLQWLGVDA
LWLPPFFQSP LRDGGYDIQD YKAILPEFGT LDEFRDLVTK AHERNMRIVI DMVLNHTSDA
HEWFQQSRED PDGPYGDFYV WRDTDEEYKN IRVIFVDTEE SNWTFDPVRR QFFFHRFFSH
QPDLNFENPA VQEAVFDVVR HWLSLGVDGL RLDAIPYLFE TEEGNGEGEP ATHDFIKRLR
RMVDDEFPGR VLIAEANQWP AETAAFFGTE EEPECHMAFD FPVMPRIFYS LRAQHAQELT
RILSETTEVP PGAAWAVFLR NHDELTLEMV SEEYRQAMYG WYAYDPRMRS NIGIRRRLAP
LLDNSRAELE LVHALLFALP GSPFLYYGDE IGMGDNIWLP DRDSSRTPMQ WTPDRNAGFS
TADPGKLFLP VVQSLVYNYN LVNVESQLAQ SRSLLHWVRN VIHVRKAHPT FGLGTMQVVE
SDHESVLSFV RSYEGSGSQV GDLPEDVLCV FSFAHNPVSV TVTAPEFAGR TLTDLFGGAQ
FPSFDEEGRV TLTLGTQAFF WLHIGDVPVV TRPAVGGAS
//
