ID G8NWY6_GRAMM Unreviewed; 670 AA.
AC G8NWY6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=AciX8_1170 {ECO:0000313|EMBL:AEU35514.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU35514.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU35514.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) 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; CP003130; AEU35514.1; -; Genomic_DNA.
DR RefSeq; WP_014264394.1; NC_016631.1.
DR AlphaFoldDB; G8NWY6; -.
DR STRING; 682795.AciX8_1170; -.
DR KEGG; gma:AciX8_1170; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_015798_0_0_0; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000007113; 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; 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; 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:UP000007113};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 211..566
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 423
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 263
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 323
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 358
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 395
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 541..542
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 481
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 670 AA; 75305 MW; CC993BDE8BA5F9C6 CRC64;
MKPSEGRRRI VIEEIQPQVD AGRYPAKRVV GDLVEVTAAI FGDGHDHVAA RLLYRHSSQR
KWSSVPFSEL SNDLWTATFS VDKLGPWNFT VEAWVDHFDT WVHDLGKRLA AQPDPKEPTQ
QTAPQDIPLA LRIGANHLDA ASSRAKGADA KALKLAAGQL RALAEANLPF YESPITAELE
ALAAKYPDLS FATKYPVELP LWVDRERARF SSWYELFPRS ASPVAGRHGT LKDVEARLPE
IAAMGFDVVY MPPIHPIGVA YRKGKNNSVT AEPGEEGSPW AIGAAEGGHT EIHPKLGTLA
DFDDLVKAAQ AQSMELALDI AFQCSPDHPW VKQHPAWFVH RPDGTIQYAE NPPKKYQDIY
PLNFESSDWR GLWDALFGVF KFWVDRGVRV FRVDNPHTKA LPFWEWCIAE VQAVAPDALF
LAEAFTRPHV MYSLAKSGFT QSYTYFTWRT DKPGLQSYFE ELTKPPVSDF FRPNVWPNTP
DILHEQLQTG GRPMFMQRVI LAATLSANYG IYGPAYELCE GRPAKPSPGK TGSEEYLDSE
KYQIREWDRS SPLSIAPLIT QLNKIRDASP ALQRNESLHF HSCPNPNLLC YSKSTPDFSD
TILVAVNLDP LNEQAGIIDL ALDKLGLPWQ GNFEVEDLLT GARYQWHDQW NYVALNPSVM
PAHVFRIVRP
//
