ID A0A1Q5E356_9ACTN Unreviewed; 568 AA.
AC A0A1Q5E356;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=AMK18_14110 {ECO:0000313|EMBL:OKJ02522.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKJ02522.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKJ02522.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKJ02522.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ02522.1}.
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DR EMBL; LISW01000002; OKJ02522.1; -; Genomic_DNA.
DR RefSeq; WP_018102566.1; NZ_LISW01000002.1.
DR AlphaFoldDB; A0A1Q5E356; -.
DR OrthoDB; 9043248at2; -.
DR Proteomes; UP000186839; 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:UP000186839}.
FT DOMAIN 31..433
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 568 AA; 65650 MW; 149E76E8F4E5B75C CRC64;
MIVNEPVHDT FEDTPAKDRD PDWFKRAVFY EVLVRSFQDS NGDGIGDLKG LTAKLDYLQW
LGVDCLWLPP FFKSPLRDGG YDVSDYTAVL PEFGDLADFV EFVDAAHQRG MRVIIDFVMN
HTSDQHEWFQ QSRTDPDGPY GDYYVWADDD KQFPDARIIF VDTESSNWTF DPVRKQYYWH
RFFSHQPDLN YENPAVQEEI ISALRFWLDL GIDGFRVDAV PYLYQREGTN CENLPETHNF
LKRVRKEIDA NYPDTVLLAE ANQWPEDVVD YFGDYGSGGD ECHMAFHFPV MPRIFMAVRR
ESRYPVSEIL AKTPAIPDNC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
IRRRLAPLLD NDRNQIELFT ALLLSLPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
DRNAGFSSSD PGRLYLPTIM DPVYGYQVTN VEASMASPSS LLHWTRRMIE IRKQNPAFGL
GTYNELPSSN PAVLAFTREH GDDLVLCVHN FSRFAQPTEL DLRSFNGRHP VELIGGVRFP
AIGQWPYLLT LAGHGFYWFR LRKDAPPS
//