ID A0A3P1UXR4_9ACTO Unreviewed; 635 AA.
AC A0A3P1UXR4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:RRD26120.1};
GN ORFNames=EII10_10295 {ECO:0000313|EMBL:RRD26120.1};
OS Actinomyces bowdenii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=131109 {ECO:0000313|EMBL:RRD26120.1, ECO:0000313|Proteomes:UP000271272};
RN [1] {ECO:0000313|EMBL:RRD26120.1, ECO:0000313|Proteomes:UP000271272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH5050 {ECO:0000313|EMBL:RRD26120.1,
RC ECO:0000313|Proteomes:UP000271272};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-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:RRD26120.1}.
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DR EMBL; RQZC01000022; RRD26120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1UXR4; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000271272; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:RRD26120.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000271272};
KW Transferase {ECO:0000313|EMBL:RRD26120.1}.
FT DOMAIN 35..430
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 570..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 70619 MW; BE936637E0EDD1D9 CRC64;
MTLTPVIPGI PALPAQDRPG LSADSEWFRT AVFYEALLRS FADSDGDGTG DLPGLISRLD
YLAWLGVDCV WIPPFYPSPM RDGGYDISDY TSIDPRYGTM EDFRELVHQA HQRGIRIVID
LVLNHTSDAH PWFQASRSDP EGPYGDFYVW RDDDSGYPDT RIIFVDSEES NWAYDVERGQ
FYWHRFFSHQ PDLNFDNPAV IEAVHDVIRF WARTGVDGFR LDAIPYLIEA EGTNCENLPG
THAIIAGIRE LLDREFPGVI TIAEANQWPQ EVVEYFGTAQ APECTMCFHF PVMPRIYYAL
REGSASAIRW VLERTPQIPA HGQWGTFLRN HDELTLEMVT DSEREQMYAW YAPEDRMRAN
VGIRRRLAPL LDASRAEIEL AHTLLMSLPG SPCLYYGDEI GMGENIWLED RDAVRTPMQW
DDSPNMGFST VVDPGALTVP LIQAPGYAHL TVATEMARPD SMLHFTRRLL HLRRAHPVLG
RGRFTLRATS DDAVLAHTRC DDPELPGAEV LLCVANLSTV PRAVTVEVPE LAGMPTTDVF
GGTAFPRIDE QGRITLTLGA RGYYWLAVGP DPQGGPQTEG DASASARIST ADGGPDEAPG
HDGPQHDERD PRAQDQPAPQ EQGAAPGHDA AQGAP
//