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Database: UniProt
Entry: A0A0W1KLF8_9ACTO
LinkDB: A0A0W1KLF8_9ACTO
Original site: A0A0W1KLF8_9ACTO 
ID   A0A0W1KLF8_9ACTO        Unreviewed;       724 AA.
AC   A0A0W1KLF8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
DE            Short=GMPMT {ECO:0000256|HAMAP-Rule:MF_02124};
DE            EC=2.4.99.16 {ECO:0000256|HAMAP-Rule:MF_02124};
DE   AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
GN   Name=glgE1 {ECO:0000313|EMBL:KTF04396.1};
GN   Synonyms=glgE {ECO:0000256|HAMAP-Rule:MF_02124};
GN   ORFNames=AQZ59_00918 {ECO:0000313|EMBL:KTF04396.1};
OS   Trueperella bernardiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Trueperella.
OX   NCBI_TaxID=59561 {ECO:0000313|EMBL:KTF04396.1, ECO:0000313|Proteomes:UP000054404};
RN   [1] {ECO:0000313|EMBL:KTF04396.1, ECO:0000313|Proteomes:UP000054404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC 89-0504 {ECO:0000313|EMBL:KTF04396.1,
RC   ECO:0000313|Proteomes:UP000054404};
RA   Bernier A.-M., Bernard K.;
RT   "Draft Genome Sequence of the Type Strain Trueperella bernardiae LCDC 89-
RT   0504T, Isolated from Blood Culture.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P) as
CC       the sugar donor to elongate linear or branched alpha-(1->4)-glucans. Is
CC       involved in a branched alpha-glucan biosynthetic pathway from
CC       trehalose, together with TreS, Mak and GlgB. {ECO:0000256|HAMAP-
CC       Rule:MF_02124}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + alpha-maltose 1-phosphate =
CC         [(1->4)-alpha-D-glucosyl](n+2) + phosphate; Xref=Rhea:RHEA:42692,
CC         Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:10183, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:63576; EC=2.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00000575, ECO:0000256|HAMAP-
CC         Rule:MF_02124};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_02124}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02124}.
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:KTF04396.1}.
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DR   EMBL; LNIZ01000003; KTF04396.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W1KLF8; -.
DR   STRING; 59561.AQZ59_00918; -.
DR   PATRIC; fig|59561.3.peg.910; -.
DR   Proteomes; UP000054404; Unassembled WGS sequence.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030979; P:alpha-glucan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd11344; AmyAc_GlgE_like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   HAMAP; MF_02124; GlgE; 1.
DR   InterPro; IPR026585; GlgE.
DR   InterPro; IPR049171; GLGE_C.
DR   InterPro; IPR021828; GlgE_dom_N/S.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR47786:SF2; AAMY DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47786; ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF21702; GLGE_C; 1.
DR   Pfam; PF11896; GlgE_dom_N_S; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02124};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_02124}; Reference proteome {ECO:0000313|Proteomes:UP000054404};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02124}.
FT   DOMAIN          257..611
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        445
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   ACT_SITE        474
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         315
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         375
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         410
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         446
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         584..585
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   SITE            531
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ   SEQUENCE   724 AA;  80768 MW;  EC5B6F8A98BBF442 CRC64;
     MTSNDFTQPA VPASAAEAAT KAPAGKAPAV AKAPAKKPAA RKPRATTRRT TKATKAAEAP
     TLGRIPIVDV QPSLQNGAWP AKGTQGEAFP VTATVFREGH DQFGAAAVLV DPEGREVQES
     IMYDSHPGLN IYKGWLTPTH PGTWEFFVRA WSDPVATWYH DADIKLNAGQ DTELVFLEGA
     RVLTRAMEKM PARSEERKIL RDAISVMKRD RVAINLRFAA ATSEDVRRAL ATYPLRDLVT
     ESARLKVNVD RERALVGSWY EFFPRSAGCY YDAAAEKWVS GTLKTAAEAL DRIAAMGFDV
     VYLTPIHPIG ETNKKGRNNS LDSIPEDPGS PYAIGSADGG HDAIHPDLGT FEDFDAFVAR
     ARELGMEVAL DIALQCSPDH PWLKEHPEWF TTRVDGTIAY AENPPKKYQD IYPLNFDNDP
     EGIYQEIKRI LKLWVSHGVT LFRVDNPHTK PVMFWKRLLE EFRAEHPEVI FLAEAFTKPP
     MLQTLGAVGF HQSYNYFAWR NEKKEIEDYL WELSAESDSR VRPAFWPTTH DILTPYMQRG
     GVPAFKIRAI LAATGSPTWG IYSGYELAEN VARPGAEEQI DNEKYEYKSR DWSSAEAFGI
     SDLLTKLNDV RSRHLALRRL RNVRINPTNN DNILCFSKVS HPEESADGSV DMVIVVLNLN
     PFETHSATID LDLSVFGTSA RWDGSPAIEV YDELTGASFR WNDRPYVNLD PNGTVAHILS
     VKVL
//
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