ID A0A1I1S1W0_9BURK Unreviewed; 1117 AA.
AC A0A1I1S1W0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ORFNames=SAMN05216321_11924 {ECO:0000313|EMBL:SFD40525.1};
OS Cupriavidus sp. OV038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1855313 {ECO:0000313|EMBL:SFD40525.1, ECO:0000313|Proteomes:UP000199583};
RN [1] {ECO:0000313|EMBL:SFD40525.1, ECO:0000313|Proteomes:UP000199583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV038 {ECO:0000313|EMBL:SFD40525.1,
RC ECO:0000313|Proteomes:UP000199583};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOKX01000019; SFD40525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1S1W0; -.
DR Proteomes; UP000199583; Unassembled WGS sequence.
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 641..991
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 687..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 822
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 851
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 689
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 749
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 784
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 823
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 966..967
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 909
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 1117 AA; 122182 MW; EE7389DB8422BDEF CRC64;
MRICQLNLTD SRAVDPEALA RTATLGFDHV LLAGWAIPHI RPDILAATFA ACRSHGLLPL
LDLALDRFPA EAAGMHDGWV DHARPGGSPD ATDSHLPGVR LRWYDEGLAP ALVAWWSAQI
REAIDAGAAG FCCRAPSRVP GRHWAEIIET AGRSSTDSTE NGGEDPVFLA FTPGTNPQQL
ADLATAPFDG AFCSLPWWDY RSAWLTEEMA RLRDFGRVLA APSLAPDGTD VLAARRALWT
AAAIGDGLMV PAGFETGAHG SAPLDTAPEA QSDGHPDDIV DAPYDLTHEL IQCNAWLAAR
DPAPAVAVRQ VSGPDAPLTV LARLPRHLAN GSNGATGPAA LIVVLNPCPI EPASFGADRV
LSALPQAAAT LQSADGGPGG TLDAAHQLDP SATITLAPAD IRLYEALPVS AQPRARRNGS
GNGNGNHRKA IDRDLATAMQ APRVAIENLA PSADHGRFAV RRTVGERVEV TADIWMDGHD
KLAAAVLWRA PGEQVWRASP MTPVINDRWR GSFPIVALGR HEFTVEAWRD TFASWLDEIG
KKRKAGVDVT LEIEEGARLV AATLDTPEGS AIPDAGALLA ELKAAAGDDA LRLEILLSPR
TETAMHAAMD TPAGRPFVSR YPTAMPVEAD RLAARFASWY ELFPRSESGD ENRHGNFDDV
IRRLPAIRAM GFDVLYFPPI HPIGQAHRKG RNNSLKAEPG DVGSPYAIGS TEGGHDALHP
QLGTFEDFQR LRRAAADHGL ELALDFAIQC SPDHPWLREH PEWFSHRPDG SLRYAENPPK
KYEDIVNVDF YAAPPGGEHL WQALRDVVMF WADQGVRIFR VDNPHTKPLP FWEWMIADVR
AKHPDTLFLA EAFTRPKMMA RLAKLGFSQS YTYFTWRNTK AELTEYMTEL TQSPLREFYR
PHFFVNTPDI NPFYLHDGGR PAFLIRAALA ALLSGLWGMY NGFEVCEGAP LVLNGVEREE
YLDSEKYQIR VRDWNQPGNI VAEISRLNQI RASHPALQDH LGVRFYHASD DAVLYFARYV
PAEPGGPAGG TSSGPTFGSD VLLAAISLDP RAPRESTIEL PLWEWGLPDH GALQAEELMS
GRRFTWTGKA QRIRLNPHEL PFALWHVRPQ QQTGDTA
//
