ID A0A1Q4DNH4_9PSEU Unreviewed; 576 AA.
AC A0A1Q4DNH4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BGP03_31030 {ECO:0000313|EMBL:OJY45903.1};
OS Pseudonocardia sp. 73-21.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY45903.1, ECO:0000313|Proteomes:UP000186163};
RN [1] {ECO:0000313|EMBL:OJY45903.1, ECO:0000313|Proteomes:UP000186163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-21 {ECO:0000313|EMBL:OJY45903.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJY45903.1}.
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DR EMBL; MKVV01000053; OJY45903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4DNH4; -.
DR STRING; 1895809.BGP03_31030; -.
DR Proteomes; UP000186163; 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 Transferase {ECO:0000313|EMBL:OJY45903.1}.
FT DOMAIN 39..441
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 576 AA; 66312 MW; A9C651248F440A3B CRC64;
MSIDTPADET LTESSSDDYG QARTLDVDHD WFKRAVFYEV LVRAFSDSNR DGTGDLKGLT
AKLDYIQWLG VDCLWLPPFY DSPLRDGGYD IRDFRTVLPE FGTVDDFVTL LDEAHKRGIR
VITDLVMNHT SDTHPWFEES RRNPDGPYGD FYMWEDDDSR YPDARIIFVD TEQSNWTYDR
VRGQFFFHRF FSHQPDLNYD NEAVQEAMLD VLRFWLDIGI DGFRLDAVPY LFARDGTNCE
NLPETHQFLK RARKVMEDEY PGRVMLAEAN QWPADVVEYF GDPEVGGDEC QMAFHFPLMP
RIFMAVRREN RFPISEILAQ TPPIPSGAQW GIFLRNHDEL TLEMVTDEER DYMYSEYAKD
PRMKANIGIR RRLAPLLEND RNQLELFTAL LMSLPGSPVL YYGDEIGMGD NIWQGDRDAV
RSPMQWTPDR NAGFSACDPG RLYLPIIMDP VYGYQAVNVE AQSHSSTSLL HWTRHMIEAR
KRHHAFGLGE YHELGGTNPS VLAYVRSHGD DVVLCVNNMS RFPQPVELDL SAWQGRSPHE
LTGGVAFPKI GELPYLLTLP GHGFYWFSIN PAEDTA
//
