GLGE_PSEAE
ID GLGE_PSEAE Reviewed; 664 AA.
AC Q9I1W4;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=PA2151;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG05539.1; -; Genomic_DNA.
DR PIR; F83376; F83376.
DR RefSeq; NP_250841.1; NC_002516.2.
DR RefSeq; WP_003113645.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1W4; -.
DR SMR; Q9I1W4; -.
DR STRING; 287.DR97_6275; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; Q9I1W4; -.
DR PRIDE; Q9I1W4; -.
DR EnsemblBacteria; AAG05539; AAG05539; PA2151.
DR GeneID; 881366; -.
DR KEGG; pae:PA2151; -.
DR PATRIC; fig|208964.12.peg.2250; -.
DR PseudoCAP; PA2151; -.
DR HOGENOM; CLU_015798_0_0_6; -.
DR InParanoid; Q9I1W4; -.
DR OMA; RPNFWPN; -.
DR PhylomeDB; Q9I1W4; -.
DR BioCyc; PAER208964:G1FZ6-2191-MON; -.
DR Proteomes; UP000002438; 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..664
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413900"
FT ACT_SITE 393
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 422
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 261
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 321
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 356
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 394
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 533..534
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 480
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 664 AA; 76330 MW; 8F59FEED54C308AD CRC64;
MSSIVRNSDD DPLVIAIQQP RIAIESVSPV VEEGAYPAKT ESDRDLRLAA RIFADGHEVL
GAEVVWRRVG ETAERRLPLL PEGNDFWSAQ LRTPPCGRLY FRIEAWIDRF AGYRRELRAK
HGARLPLDLE LREGDELLQR CAERGGPEIA AACAPLAERL QACQSVEERV ALWLAAQTGE
LLRLVGPREH LVRSREYPVE VERPLARFAS WYELFPRSES GDPTRHGTFD DVIRRLPQIA
AMGFDVLYFP PIHPIGRTHR KGRNNSLRAE AGDPGSPYAI GSEEGGHEAI HPELGDREDF
RRLLVAVREH GMELALDFAI QCSPDHPWLR EHPGWFAWRP DGSLRYAENP PKKYEDIVNV
DFYAEQALPS LWEALRDVVL GWVEQGVTLF RVDNPHTKPL PFWEWLIAEV RGRHPQVIFL
SEAFTRPAMM ARLGKVGFSQ SYTYFTWRND KQELAEYFAE LNQPPWRDCY RPNFFVNTPD
INPWFLQRSG RPGFLIRAAL ATMGSGLWGM YSGFELCEAA ALPGKEEYLD SEKYQLRPRD
YQAPGNIVAE IARLNRIRRE NPALQTHLGF QAYNAWNDRI LYFGKRTADL ANFVLVAVCL
DPHEAQEAHF ELPLWEFGLP DDASLQGEDL MNGHRWVWHG KVQWMRIEPW HLPFGIWRVR
RVDA
