ID A0A0D5CIB7_9MICO Unreviewed; 577 AA.
AC A0A0D5CIB7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=VO01_07805 {ECO:0000313|EMBL:AJW79045.1};
OS Clavibacter michiganensis subsp. insidiosus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Clavibacter.
OX NCBI_TaxID=33014 {ECO:0000313|EMBL:AJW79045.1, ECO:0000313|Proteomes:UP000032604};
RN [1] {ECO:0000313|EMBL:AJW79045.1, ECO:0000313|Proteomes:UP000032604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1-1 {ECO:0000313|EMBL:AJW79045.1,
RC ECO:0000313|Proteomes:UP000032604};
RX PubMed=25953184;
RA Lu Y., Samac D.A., Glazebrook J., Ishimaru C.A.;
RT "Complete Genome Sequence of Clavibacter michiganensis subsp. insidiosus
RT R1-1 Using PacBio Single-Molecule Real-Time Technology.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CP011043; AJW79045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D5CIB7; -.
DR KEGG; cmh:VO01_07805; -.
DR PATRIC; fig|33014.5.peg.1623; -.
DR HOGENOM; CLU_006462_2_1_11; -.
DR Proteomes; UP000032604; Chromosome.
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}.
FT DOMAIN 30..430
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 577 AA; 66217 MW; 4ECF89B13A08047E CRC64;
MRRTVSFTAP ITLPGLTLDK QWYKRSVFYE VMIRSFVDSN GDGTGDIQGL ISKLDYLQWL
GIDGLWLPPF FQSPLRDGGY DISDYLAVLP EFGTLDDFKE LVTKSHERNM RIVIDLVMNH
TSDQHEWFQQ SRSDPDGPYG DFYVWSDTDE KYEDIRVIFV DTEESNWTFD PVRRQFFFHR
FFSHQPDLNF DNPKVHEAIY GVIRHWLDMG VDGLRLDAIP YLYETEEGNG EGEPATHEFL
KRLRAMVDEE YPGRILIAEA NQWPREVSAF LGTEEEPECH MAFDFPIMPR IFYSLRSQTA
DELKRIMGET FEIPEAAAWG VFLRNHDELT LEMVSEEYRQ AMYGWYAYDP RMRVNIGIRR
RLAPLLDNSR AELELVHALL FSLPGSPFLY YGDEIGMGDN IWLPDRDASR TPMQWTPDRN
AGFSTADPGK LYLPVVQSLV YNYAQINVES QLAQSRSLLH WVRNVIHVRK AHPVFGQGTI
RVLPTDHESV LAFVRSYEGS GTHFGDRAED VLCVFSFAHN PVSVTIDASD FAGSQLYDLF
GGGVFPTVGD DGRLTLTLAT QSFYWLHMGA PAIGGRP
//
