ID A0A158H4U8_9BURK Unreviewed; 1126 AA.
AC A0A158H4U8;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-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=AWB65_02907 {ECO:0000313|EMBL:SAL39167.1};
OS Caballeronia humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL39167.1, ECO:0000313|Proteomes:UP000054977};
RN [1] {ECO:0000313|EMBL:SAL39167.1, ECO:0000313|Proteomes:UP000054977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL39167.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCNW02000013; SAL39167.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158H4U8; -.
DR STRING; 326474.AWB65_02907; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000054977; 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 668..995
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 848
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 877
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 716
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 776
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 811
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 849
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 988..989
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 935
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 1126 AA; 125851 MW; 2D5BF109C75DB78D CRC64;
MENHPAHHAY APRIYFIDPL LVGPLPKWPA HFEHAAALGF DHILIGSPFV PGANGHRQAI
SDHHRLHPVF ESDEPAAAGL AKLADAAKKH GLTLLVDVVI DRVSADGGLF HENKHWFHPF
ESAEARLDPR HAPREENVAH ANFGDAEAAQ HLTEWWAREL LLLADAGIGG FRFDAPHKVP
AHVWRRLGAA VRERHPETRW LAWTVGISRH DLHGLTDAGF DAVFSSSRWW DYQSAWLADE
HAALVRVAPP ISFPEEPFGT RLLSDLPDTG DTALVERAYQ RALYAAAAIG TGILVPMGFE
YGVGLPMSYQ YGVAAEYDRA QSQARFDLSK DVARANALQR DTGTLATTGE LRSLTGAGTH
FAALVRANGP DLRNANAAAF IVINPDLATP VRVDPLHLLE AVPGNFTRFA PLGDAKATPA
PLAEFTLGAG EARMFRASAE PYVLLAQPQV KRGAKTADKK SVAEAITNPR VAIESVTPSV
DHGRFPAKRI VGEAVEVRAA IFAEGHDKIA AAVQWRAADE TDWHEAPMVP VLPLGNDLWT
TLIPLDRVGR HEFTVMAWRD DFASLVDHMQ KKLKAGQTVE LELEEARHLF ALMLAEVQTV
EEAEKEPLDS IVKEFTKADA DRRLELVLAE ATAKAVADAR HRPFLSRDPV IYRVDAERAA
ARFASWYEIF PRSMSDDENR HGTFVDVIGK MPRIRDMGFD VLYFPPINPI GMANRKGKNN
SLTAQPGDVG SPYAIGGKEG GHTAVHPELG TLEDFRQMLD AAHAHGLEIA LDFAVQCSPD
HPWLKEHPTW FAWRPDGTLR YAENPPKKYQ DIVNPDFYAK DAKPELWVSL RDVFLFWIAA
GVKIFRVDNP HTKPFPFWEW AINDVRARHP DVMFLAEAFT RPRVMNRLAK LGFSQSYTYF
TWRETKRDFI EYMHDLTQTD AKEFFRPNFF VNTPDINPRF LQRSGRAGFV IRAALAATLS
GLWGVYSGFE LCEAAALPNS EEYLDSEKYQ LRAWDWNRPG NIVGEVTLLN RIRRANPALQ
THLGINFLPA HNEHILFFEK SNAAGDNVVL VAINLDPFNE QGADVDLPWA TLERWGVKEW
DAVAVEDQVT GQRFQWTGRR QHVRLDPNSL PFAVWRIAPA WGLPKP
//
