ID A6DPQ0_9BACT Unreviewed; 654 AA.
AC A6DPQ0;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=glgE {ECO:0000256|HAMAP-Rule:MF_02124};
GN ORFNames=LNTAR_19777 {ECO:0000313|EMBL:EDM26345.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM26345.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM26345.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM26345.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EDM26345.1}.
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DR EMBL; ABCK01000017; EDM26345.1; -; Genomic_DNA.
DR RefSeq; WP_007279831.1; NZ_ABCK01000017.1.
DR AlphaFoldDB; A6DPQ0; -.
DR STRING; 313628.LNTAR_19777; -.
DR eggNOG; COG0366; Bacteria.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000004947; 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:UP000004947};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 210..554
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 389
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 418
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 258
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 353
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 390
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 529..530
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 476
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 654 AA; 75667 MW; AF6569CF765D4E4F CRC64;
MSQELLRTDY NSHYVYIQNV KPSIDGGIYP IKRRQGDQVN VSAEILQQGH DGLSAELHFK
HKSERRWQSI PMDCENAGLD LYKAQFTVEN MGLYEFKIFA YADFYDNWAH GVEKKFNVGE
DIASELIEGV ELLKDCQSRA NKTVAKNLAS IVKELEAEKD MSRKFYRMME GELKDLAASL
PDKESFNTAT SSIYSVRCDR RRAEFASWYE VFPRSCSGKE GMHGTFRDVE KMLPYIDDLG
FDVLYFTPIH PIGFSKRKGK NNSLTSAKGE PGSPYAIGSE AGGHFAVHPE LGTMDDFDHL
VKACAEKDIE IALDFALNCS PDHPYLKEHP DWFYRRPDGS IKYAENPPKK YEDIYPLNFE
CEDRKNLWAE IRDIFLFWAS HGVRTFRVDN PHTKPISFWN WCIAEVHKEY EDVIFLSEAF
TRPRLMELLA KNGFTQSYSY FTWREGKEEL TEYFNYLHNS EAVEYMTANI FATTPDILPK
HLQFSSAQMF RIRHALAVTL SPMYGMYTGY ELCENIPVGP RDELMDSEKY ELKVRNYEDS
GSIAPFVKKL NMIRRENPAL QVQNNLKFCS VNNEKLIAYI KRVEGNTLLI VVSLDPLHTQ
SGMVHLPLHE LGFDQHHQYK MHDLMTDQVY DWSGPDNFVE LSDRAAPVHV FRVF
//
