ID B3Q5R7_RHIE6 Unreviewed; 1075 AA.
AC B3Q5R7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=RHECIAT_PC0000470 {ECO:0000313|EMBL:ACE94548.1};
OS Rhizobium etli (strain CIAT 652).
OG Plasmid pC {ECO:0000313|EMBL:ACE94548.1,
OG ECO:0000313|Proteomes:UP000008817}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE94548.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE94548.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE94548.1,
RC ECO:0000313|Proteomes:UP000008817};
RC PLASMID=Plasmid pC {ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) 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; CP001077; ACE94548.1; -; Genomic_DNA.
DR AlphaFoldDB; B3Q5R7; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; rec:RHECIAT_PC0000470; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_007336_1_2_5; -.
DR Proteomes; UP000008817; Plasmid pC.
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; 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}; Glycosidase {ECO:0000313|EMBL:ACE94548.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02124}; Hydrolase {ECO:0000313|EMBL:ACE94548.1};
KW Plasmid {ECO:0000313|EMBL:ACE94548.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 624..969
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 109..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 804
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 833
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 672
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 732
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 767
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 805
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 944..945
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 891
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 1075 AA; 120523 MW; BB0FA4097CCAB0F5 CRC64;
MLLSAKQGAV STPPRIYYVN PLLLQGIDAW REVFDHAADT GFDHVLTAPL FDRGGERSVF
TSQDVNRLDP QLQLGSTVED GVARLAEAAG KSGVGLMMDL MLDGKRQDRQ AGFRPVDPRR
SPLDPAEPMS MLEAERQSQL SVEWVERLQR LSDAGLAGYR VLGIDRATPA LFKTLIAGVH
EKAEVQFFAW TPGTDFAVRS AIADAGFAGC FSSMAWWDLD ERWFVEEHHI QEPFGWQIAF
PEPPFARRIA HGTESREILE RRAVRALRLA ASLGGGLMVP MGFEYGAATP LDPTHGDGSG
LRRLRHDLAF DISSEIRLAN SEIGKAGQMR APSLRLIRNA NGPVSVLVQS EAEDLRSASD
VRFILLNRDL RRSAPAPVTA LREAAAGFLP VTADGAALRL RAGEIRVIEG QVPEPITSRP
ALDIEQATAS ARLAIENIVP RVDDGRFPVK RVVGETVTVE ADIFADGHDP LAAALLWRPH
DAIAEWNETP MQLVGNDRWR AEFLLERMGR YEFAVEAWKN PFAIFRYELT KKNDARLDLK
LELQEGLNLV RAAKAEAPAA LGAGLQALID SLEKASDPER TAILLDPETS ELMNKADRRP
FRLRSTASAV DAERKEAAFA SWYQIFPRSQ SGDPNRHGTF DDVIPRLADI RGMGFDVLYF
PPIHPIGSTN RKGRNNSLKA APGDPGSPYA IGSEDGGHDA IHPELGDFED FGRLVEEAGR
HGLEIALDLA IQASPDHPWL REHPGWFDWR PDGTIKYAEN PPKKYEDIVN VDFYTKDALP
SLWVELRDIV QLWVDQGVKL FRVDNPHTKP FPFWEWLIGD IRARHPDVVF LSEAFTKPKV
MYRLAKIGFS QSYTYFTWRN AKWELEEYMR ELTETAPKEF FRPHFFVNTH DINPDFLQNA
PRPAFLIRAA LAATLSGLWG VYNGFELCEG RPDAKRKEYA DSEKYEIRVW DYDRPGNIIA
EIRMLNRIRN ENIALHSHLG LTLLPASNDN ILFFEKASRA RDNVLLIAIS LDPHNFQQSD
VELPLWKWSL GDGGALDAED LVGGHRFKWT GKRQTVALNP HILPFAIWRV RAAEA
//
