GLGE_CERS4
ID GLGE_CERS4 Reviewed; 668 AA.
AC Q3J3M8;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 93.
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=RHOS4_10380;
GN ORFNames=RSP_2445;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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: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; CP000143; ABA78606.2; -; Genomic_DNA.
DR RefSeq; YP_352507.2; NC_007493.2.
DR AlphaFoldDB; Q3J3M8; -.
DR SMR; Q3J3M8; -.
DR STRING; 272943.RSP_2445; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABA78606; ABA78606; RSP_2445.
DR KEGG; rsp:RSP_2445; -.
DR PATRIC; fig|272943.9.peg.1364; -.
DR eggNOG; COG0366; Bacteria.
DR OMA; RPNFWPN; -.
DR Proteomes; UP000002703; Chromosome 1.
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..668
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413902"
FT REGION 263..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 395
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 424
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 264
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 324
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 359
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 396
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 535..536
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 482
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 668 AA; 76701 MW; 8470F5E4B38CCADB CRC64;
MAAATGAQDR RDGGEEALMR LADARVAIEG VNLEIDGGRF AAKVVAGWEV AVEADIFCDG
HDSIDAAVLH RQRGTDDWIE VRMEFLVNDR WQAHVTFAEN AFHELTFLAW RDLYTTWRKE
VAKKLAAGQK IDLELEEGRR LLQSVETAGA EDRALVDRIL GEDGADQEAG ARFARMSSPE
AVAAMKRCAP RTNLTCYKIL PIFADREAAA FSAWYEMMPR SQSDDPERHG TFDDVIRKLP
YVRDLGFDVL YFTPIHPIGR VNRKGRNNSL TPAPDDPGSP YAIGSEEGGH DAIHPELGDF
ESFGRLVEAA HAHGLEIALD FAIQCAPDHP WIREHPEWFD WRPDGTIKFA ENPPKKYEDI
VNVHFYRGAL PELWYALRDV VLFWVEKGVK IFRVDNPHTK PFPFWEWMIG EVQSQHPDVI
FLAEAFTRPK VMKRLGKVGY GQSYSYFTWR NTKAELIDYL TELTTEECRH YMRPNFFANT
PDINPVYLQH SGRAGFRVRL ALAATLGGNY GLYNGYEICE ATPVPGKEEY FNSEKYQLRA
WDFDQPGHIQ DDIRLMNHIR RTHPAMRDFT RLRFYDAHND SVLAYGKSTE DKQDFLLFHV
NLDPHAAQTF EFEVPLWEFG LPDDASVEVE DLLNGNRFTW HGKWQWLELD PQTRPYAVWR
LYAPGMPR
