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
//