GLGE_BIFLO
ID GLGE_BIFLO Reviewed; 746 AA.
AC Q8G784;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
DE Short=GMPMT {ECO:0000255|HAMAP-Rule:MF_02124};
DE EC=2.4.99.16 {ECO:0000255|HAMAP-Rule:MF_02124};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
GN Name=glgE {ECO:0000255|HAMAP-Rule:MF_02124}; OrderedLocusNames=BL0388;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_02124};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02124}.
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DR EMBL; AE014295; AAN24224.1; -; Genomic_DNA.
DR RefSeq; NP_695588.1; NC_004307.2.
DR RefSeq; WP_007054760.1; NC_004307.2.
DR AlphaFoldDB; Q8G784; -.
DR SMR; Q8G784; -.
DR STRING; 206672.BL0388; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAN24224; AAN24224; BL0388.
DR GeneID; 66504471; -.
DR KEGG; blo:BL0388; -.
DR PATRIC; fig|206672.9.peg.1130; -.
DR HOGENOM; CLU_015798_0_0_11; -.
DR OMA; RPNFWPN; -.
DR PhylomeDB; Q8G784; -.
DR Proteomes; UP000000439; Chromosome.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_02124; GlgE; 1.
DR InterPro; IPR026585; GlgE.
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; PTHR10357:SF203; PTHR10357:SF203; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..746
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413892"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 343
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 403
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 438
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 474
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 612..613
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 559
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 746 AA; 82905 MW; B56C9717A80D96E1 CRC64;
MAAVQHRATT RTSNTDNSTT KTKSKATSAR KSPATKRKRV SAETARAAAA LKGLAVEAPA
PSIEANEPGQ FGRINVMDIT PAEERGIFPA RVELGEPFEM TAQVFIEGRT KVGATAIVRN
PRGKETMRRA MTCVNPGLDR WTVMVKCGEH SDLKPWEDGY AAVKRQLGEW TVTIEGWEDA
YVSWLHDARI KVRVMDDVDN ALNSGAELLA RWAETPDTGL TARDRKTLEK AAETMADQTL
SAEDRLAAGD NPTIAALHET HPLRDGISPS QPQRFKVERP KSSFAAWYQF FPRSEGATID
PNTGKIIQGT LKTSMAGLER AAAEGFDIVY LPPVFPIGVT NRKGRNNTLV AGPDDPGSPF
GIGSELGGHD TVDPLLGTMD DFKALCQRAH ELGLEIALDF ALQCSPDHPW VKAHPNWFRH
KPDGSIAFAE NPPKKYQDIY PIDFNADMPG IEKEVERIMN LWIEAGVTIF RIDNPHTKPV
RFWQDVIAAV TKKHPEILFL AEAFTRPGMM RALSYVGFTQ SHCYFPWRNT KDELEEYLPV
TNGDDGYYQH NTFWPTTPDI LTAYVRDNGV AGHCVRAVLA AMGSPSWGIY NGYELIENKQ
RPGFEEQIDN EKYEVKVRDW SKAKQYGVAE MLTALNKIRR AHPAALSYHN LTVLPTSDPN
ILAFARHTPA ELTGTGQADT LIVVVNLDGH NAHQSMIHLE LSELGLPTDR PLNVRDELTG
REFQWGWDNY VSLAPWADVA HILSVQ
