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Database: UniProt
Entry: A0A2V1HVP8_9MICO
LinkDB: A0A2V1HVP8_9MICO
Original site: A0A2V1HVP8_9MICO 
ID   A0A2V1HVP8_9MICO        Unreviewed;       574 AA.
AC   A0A2V1HVP8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
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:PVZ94447.1};
GN   ORFNames=DDQ50_12105 {ECO:0000313|EMBL:PVZ94447.1};
OS   Amnibacterium flavum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Amnibacterium.
OX   NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ94447.1, ECO:0000313|Proteomes:UP000244893};
RN   [1] {ECO:0000313|EMBL:PVZ94447.1, ECO:0000313|Proteomes:UP000244893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ94447.1,
RC   ECO:0000313|Proteomes:UP000244893};
RA   Tuo L.;
RT   "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
RL   Submitted (MAY-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:PVZ94447.1}.
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DR   EMBL; QEOP01000002; PVZ94447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1HVP8; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000244893; 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:UP000244893};
KW   Transferase {ECO:0000313|EMBL:PVZ94447.1}.
FT   DOMAIN          26..426
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   574 AA;  65648 MW;  C8E298FDFAF9B23A CRC64;
     MSFTAPITLP GLALNPQWYR RSVFYEVMVR SFADSNGDGT GDLGGLTARL DYLQWLGIDA
     LWLPPFYQSP LRDGGYDVSD FKSVLPEFGT IDEFRELVKK AHERNMRIVM DFPLNHTSDA
     HEWFQQSRED PEGPYGDYYV WSDTDEKYDN IRIIFVDTEE SNWTFDPVRR QFFFHRFFSH
     QPDLNFENPA VQEAIFDIVR FWLDLGVDGL RLDAIPYLYE SEGGNGEGEP ATHEYIKRLR
     AMIDRDYPGR ILIAEANQWP REVAAFFGTE EEPECHMAFN FPIMPRIFYS LRAQTATELV
     RILGETTDVP VGAAWGVFLR NHDELTLEMV SEEYRQAMYG WYAYDPRMRS NIGIRRRLAP
     LLDNSRAELE LAHALLFSLP GSPFLYYGDE IAMGDNIWLP DRDASRTPMQ WTPDRNAGFS
     SADPGKLFLP VVQSLVYNYT LVNVEAQLAQ SRSMLHWVRN VIHTRKAHPT FGLGSLEVQD
     TDHESALAFV RSYEGASTGA QHMGDVAEDV LCVFNFSHNP ITVKVTMADH AGARLTDLFG
     GGEFPRVADD GTVTFTLGSQ AFYWLKIWDP SAQF
//
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