ID Q0B3Y6_BURCM Unreviewed; 1136 AA.
AC Q0B3Y6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
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 OrderedLocusNames=Bamb_5590 {ECO:0000313|EMBL:ABI91137.1};
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670 {ECO:0000313|EMBL:ABI91137.1, ECO:0000313|Proteomes:UP000000662};
RN [1] {ECO:0000313|Proteomes:UP000000662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD {ECO:0000313|Proteomes:UP000000662};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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}.
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DR EMBL; CP000442; ABI91137.1; -; Genomic_DNA.
DR RefSeq; WP_011660496.1; NZ_CP009800.1.
DR AlphaFoldDB; Q0B3Y6; -.
DR GeneID; 69548533; -.
DR KEGG; bam:Bamb_5590; -.
DR PATRIC; fig|339670.21.peg.6515; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000000662; Chromosome 3.
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; 2.
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; 2.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 662..1007
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 842
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 871
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 710
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 770
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 805
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 843
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 982..983
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 929
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 1136 AA; 124619 MW; 19D446740458FB01 CRC64;
MNPTPPFAPH IYFCDARLVG PLDAWPDTFQ HIAGMGFDHV LIGGFWAASV AGFPRHVADF
HRPAATFATR AGALETFSRL AQLAHGHGLR VLLEVVPDRI ARDNPLRTEH PDWYVERAHD
DALIDPRSAA HEMDVAHAQV GEDAAHDALS AWWCTHLATF ADAGASGFLI DAPHHLPAAW
WPGWRAALRR ARPDVAVLAG VPGHARDALA QLEAAGFDAV FSSVRWWDLH APWFVDEHRL
LRRIGSPIAF PDAIDGPRLA DNWNTAPDET VARAYHRALW TAAAVGTGWL VPMGFERGVT
LPLMARDADA ARFRAALDDA RFDLSGAIAD ANAWRRATPL AAERGEIAQL SAPGARATAL
LRGSGPSLEH DDTALLIALN PDLDAPTHVD PATILPGVPG GFTHVSPPNG ARKSAPAAPA
APVALQAFTL EPGGYALLDA RRAPPALART DAAGERTALS AALAADRIAI ERVEPAVDGG
RFAIKRVIGE TLVVHASIFT DGHAHLAAAL QWRADDEDAW REVPFVAEPN DRWHACISLD
RLGRHAFRVI AWRDDWASLV TDITKKRAAG QDVTLELREA QLLLATALKH ADAVDRRART
RMEQLTAEFN DAAPDKRLEL LGAPALADAY AALRYRPFVT HDDAVYPVDV ERRAARFSSW
YEMFPRSASN DPHRHGTFDD VIAQLPRIRD MGFDVLYFPP IHPIGTTARK GRNNTLTAGP
DDVGSPYAIG SPEGGHTAVH PQLGTLASFR TLVDAAHAQG LEIALDFAIQ CSPDHPWLAA
HPGWFAWRPD GSLRYAENPP KRYQDIVNPD FYAPDALPDL WVALRDAVLF WVDAGVRIFR
VDNPHTKPLP FWAWMIADVR GKHPDVVFLS EAFTRPGMMY RLAKVGFSQS YTYFTWRETK
REFIDYLTEL TAGPAREFFR PNFFVNTPDI NPRHLQNAPR SQFVIRAALA ATLAGSWGLY
SGFEIGESAP LPDSEEYADA EKYELRVRDW RKAAHIGGEI ARLNRARRDH PALQTHLGLT
FVDADNDQVL VFVKATPAHD SVVAVAISLD PWHPQAANFT LDAALWRGFG LVDGEPLDAL
EQDAAHAETW RGHRQYVSLD PHVRPYAIWR LAPSPGAARA AAPDPADARG HSGAHG
//
