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Database: UniProt
Entry: A0A255H0B2_9ACTN
LinkDB: A0A255H0B2_9ACTN
Original site: A0A255H0B2_9ACTN 
ID   A0A255H0B2_9ACTN        Unreviewed;       583 AA.
AC   A0A255H0B2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
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:OYO19454.1};
GN   ORFNames=CGZ93_12975 {ECO:0000313|EMBL:OYO19454.1};
OS   Enemella dayhoffiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Enemella.
OX   NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO19454.1, ECO:0000313|Proteomes:UP000216311};
RN   [1] {ECO:0000313|EMBL:OYO19454.1, ECO:0000313|Proteomes:UP000216311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML 130396 {ECO:0000313|EMBL:OYO19454.1,
RC   ECO:0000313|Proteomes:UP000216311};
RA   Bernier A.-M., Bernard K., Domingo M.-C.;
RT   "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL   Submitted (JUL-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:OYO19454.1}.
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DR   EMBL; NMVQ01000034; OYO19454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A255H0B2; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000216311; 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:UP000216311};
KW   Transferase {ECO:0000313|EMBL:OYO19454.1}.
FT   DOMAIN          16..434
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   583 AA;  66878 MW;  A54ABB57645305FB CRC64;
     MDPEDHEWFK KAVFYEVMVR SFRDSNGDGV GDFAGLAEKL DYLQWLGVDC LWLPPFFPSP
     LADGGYDVAD YTGVLPVLGT VEEFRAFIEG AHERGIRIII DFVMNHTSDQ HPWFQQSRSD
     PDGPYGDYYV WSDGGPLEGQ VPEAYSDARI IFVDTEASNW SYDEVRGQYF WHRFYSHQPD
     LNFENPKVLA EMLDAIRFWL RMGIDGFRLD AVPYLIEEDG TNCENLDGTH RILKAVRRMV
     DTEFPGRILL CEANQWPHDV VEYFGNDDEC QMAFHFPVMP RLYMGLRQES RACISDILAD
     TPPIPTGCQW GTFLRNHDEL TLEMVSDEDR EYMWTEYAPD PRMKCNIGIR RRLAPLVDGD
     LKRVHLLHAM LLGLPGSPVL YYGDEIGMGD NIWLHDRDGV RTPMQWSAED GAGFSTADED
     SFYLPLIQDP RYAKEGVNVE QQMLDPGSLL VWLRAMLVIR RNHPVFGLGD FTDLGGDNEK
     VFSFLRSHRD ESGQRISVLC VNNLSAEPQT TKLDLSRFRG LVPFDLLRDD DHHPIDTETA
     HDYSIDVAGH GFLWLRIMAD DPDLAHAEEI AQHEREEDHD DIA
//
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