ID   Q88FM9_PSEPK            Unreviewed;       661 AA.
AC   Q88FM9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   10-JUN-2026, entry version 129.
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   ECO:0000313|EMBL:AAN69650.1};
GN   OrderedLocusNames=PP_4060 {ECO:0000313|EMBL:AAN69650.1};
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pseudomonadales; Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN69650.1, ECO:0000313|Proteomes:UP000000556};
RN   [1] {ECO:0000313|EMBL:AAN69650.1, ECO:0000313|Proteomes:UP000000556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC   {ECO:0000313|Proteomes:UP000000556};
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA   Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA   Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA   Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA   Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA   Dusterhoft A., Tummler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
RN   [2] {ECO:0000313|EMBL:AAN69650.1, ECO:0000313|Proteomes:UP000000556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC   {ECO:0000313|Proteomes:UP000000556};
RX   PubMed=26913973; DOI=10.1111/1462-2920.13230;
RA   Belda E., van Heck R.G., Lopez-Sanchez M.J., Cruveiller S., Barbe V.,
RA   Fraser C., Klenk H.P., Petersen J., Morgat A., Nikel P.I., Vallenet D.,
RA   Rouy Z., Sekowska A., Martins Dos Santos V.A., de Lorenzo V., Danchin A.,
RA   Medigue C.;
RT   "The revisited genome of Pseudomonas putida KT2440 enlightens its value as
RT   a robust metabolic chassis.";
RL   Environ. Microbiol. 18:3403-3424(2016).
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=alpha-maltose 1-phosphate + [(1->4)-alpha-D-glucosyl](n) =
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:ARBA00048735, 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; AE015451; AAN69650.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q88FM9; -.
DR   STRING; 160488.PP_4060; -.
DR   PaxDb; 160488-PP_4060; -.
DR   KEGG; ppu:PP_4060; -.
DR   PATRIC; fig|160488.4.peg.4317; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_015798_0_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   PhylomeDB; Q88FM9; -.
DR   BioCyc; PPUT160488:G1G01-4325-MONOMER; -.
DR   Proteomes; UP000000556; 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   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; IPR017853; GH.
DR   InterPro; IPR006047; GH13_cat_dom.
DR   InterPro; IPR026585; GlgE.
DR   InterPro; IPR049171; GLGE_C.
DR   InterPro; IPR021828; GlgE_dom_N/S.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR47786; ALPHA-1,4-GLUCAN:MALTOSE-1-PHOSPHATE MALTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR47786:SF2; GLYCOSYL HYDROLASE FAMILY 13 CATALYTIC DOMAIN-CONTAINING PROTEIN; 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:UP000000556};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02124}.
FT   DOMAIN          211..556
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          262..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        391
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   ACT_SITE        420
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         259
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         319
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         354
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         392
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   BINDING         531..532
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT   SITE            478
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ   SEQUENCE   661 AA;  75542 MW;  4998167145DED70F CRC64;
     MANDHPDQAI SLAQALLAPR IVIEDTQPVL DAGSFAAKAV SGQPVAVSTK AYSDGHDRLA
     VMLNWRQAHS RRWHCVPMQS AGNDLWQAEF TPTELGPHRF SIEAWIDPFA TYCHDLEKKY
     HAGVEVKLEL EEGRLMLGKG IELCSGALRE ALEAVQSRLA TLSTDDQVAV FLDPTTARLM
     GEAEHRSYLT RSPDFPLDVD RPAALFASWY ELFPRSITDD PQRHGTFNDV HERLPMIRDM
     GFDVLYFPPI HPIGMQHRKG RNNALKAEPG DPGSPYAIGS PEGGHEAIHP QLGSRDDFRR
     LVAAAAEHGL EIALDFAIQC SQDHPWLKEH PGWFSWRPDG TIRYAENPPK KYQDIVNVDF
     YAPEAVPSLW LALRDVVVGW VEEGVKTFRV DNPHTKPLPF WQWLIANVRS QHPDVIFLAE
     AFTKPAMMAR LGKVGYAQSY TYFTWRNHKQ ELREYFEQLN QPPWSQCYRP NFFVNTPDIN
     PFFLHTSGRA GFLIRAALAT MGSGLWGMYS GFELCEGTPL PGKEEYLDSE KYEIRPRDFT
     QPGNIIAEIA QLNRIRRQNR ALQTHLGVAF FNCWNDNILY FAKRTPERDN YILVAVSLDP
     HNAQEAHFEL PLWELGLDDN AETQGEDLMN GHRWSWYGKT QWMRIEPWHL PFGIWRIEKA
     R
//