ID A0A0Q5CGZ3_9MICO Unreviewed; 582 AA.
AC A0A0Q5CGZ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=ASF54_01025 {ECO:0000313|EMBL:KQQ27423.1};
OS Frondihabitans sp. Leaf304.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=1736329 {ECO:0000313|EMBL:KQQ27423.1, ECO:0000313|Proteomes:UP000051456};
RN [1] {ECO:0000313|EMBL:KQQ27423.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27423.1,
RC ECO:0000313|Proteomes:UP000051456};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ27423.1, ECO:0000313|Proteomes:UP000051456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf304 {ECO:0000313|EMBL:KQQ27423.1,
RC ECO:0000313|Proteomes:UP000051456};
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:KQQ27423.1}.
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DR EMBL; LMNV01000002; KQQ27423.1; -; Genomic_DNA.
DR RefSeq; WP_055957706.1; NZ_LMNV01000002.1.
DR AlphaFoldDB; A0A0Q5CGZ3; -.
DR STRING; 1736329.ASF54_01025; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000051456; 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:UP000051456}.
FT DOMAIN 26..426
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 582 AA; 66333 MW; 93C8FD34B89B66BE CRC64;
MSFTAPIQTP GLTLDPQWYR RSVFYEVMVR SFVDSNGDGA GDIAGLSSRL DYLQWLGIDA
LWMPPFFQSP LRDGGYDISD YKAILPEFGT LDEFRDLVTK AHERNMRIVI DMVINHTSDA
HDWFQQSRED PDGPYGDFYT WSDTDEKYEN IRIIFVDTEE SNWTFDPVRR QFFFHRFFSH
QPDLNYENPK VHEAIYDVIR HWLDLGVDGI RLDAIPYLYQ SEEGNGEGEP ATHEFVKKLR
AMIDEEYPGR IMIAEANQWP REVAAFFGTE DEPECHMAFD FPVMPRIFYS LRSQDAGELT
RILSETTDVP ESAGWGVFLR NHDELTLEMV SEEYRQAMYG WYAYDPRMRS NIGIRRRLAP
LLDNSRAELE LAHALLFALK GSPFLYYGDE IGMGDNIWLN DRDASRTPMQ WTPDRNAGFS
TADPGKLYLP TIQSLVYNYT LVNVESQLAQ SRSLLHWIRN VIHVRKAHPT FGLGTLDVLP
TNHESTLAFV RSYAGSGTQF GDSAEDILCV FSFAHNPTSV TVSAPQFAGR TLFDLFGGGQ
FPSFDEKGEV TLTLGTQAFF WLHVGGPDTA TTDDQAAVSA QG
//
