ID I0RQI3_MYCXE Unreviewed; 699 AA.
AC I0RQI3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=MXEN_10246 {ECO:0000313|EMBL:EID13386.1};
OS Mycobacterium xenopi RIVM700367.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID13386.1, ECO:0000313|Proteomes:UP000003584};
RN [1] {ECO:0000313|EMBL:EID13386.1, ECO:0000313|Proteomes:UP000003584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID13386.1,
RC ECO:0000313|Proteomes:UP000003584};
RX PubMed=22628510; DOI=10.1128/JB.00482-12;
RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA van Soolingen D., Bitter W., Pain A.;
RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL J. Bacteriol. 194:3282-3283(2012).
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 -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC {ECO:0000256|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EID13386.1}.
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DR EMBL; AJFI01000060; EID13386.1; -; Genomic_DNA.
DR AlphaFoldDB; I0RQI3; -.
DR PATRIC; fig|1150591.3.peg.2054; -.
DR OrthoDB; 9805159at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000003584; 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 GO; GO:0005978; P:glycogen 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; 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}; Glycogen biosynthesis {ECO:0000256|HAMAP-Rule:MF_02124};
KW Glycogen metabolism {ECO:0000256|HAMAP-Rule:MF_02124};
KW Glycosidase {ECO:0000313|EMBL:EID13386.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_02124}; Hydrolase {ECO:0000313|EMBL:EID13386.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 230..571
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 416
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 445
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 286
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 346
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 381
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 417
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 555..556
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 501
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 699 AA; 78201 MW; 993B47EAEBEC0405 CRC64;
MEWRVPGRVE IDDVQPVVSC GTYPAKAVVG EVVPVRAAVW REGHEAVAAT LVVRYLGPRY
PQVSELRRVK AVQLADQVPT ATPEAPTRVK PLLVPMTMGE EPFIFHGQFT PDSVGLWTFR
VDGWGDPIRS WRDAVVAKLD AGQGETELSN DLLVGARLFD RAAAGVPRAE RDPLLAAAAA
LRTPGDPVTR AALALSPQID ELLRRYPLRE LVTRGEQFGI WVDRPLARFG AWYEMFPRST
GGWDEDGNPV HGTFATAAAA LPRIANMGFD VVYLPPIHPI GKVHRKGRNN AATAAPGDVG
SPWAIGSDEG GHDAVHPLLG TLDDFDDFVS TARDLGLEVA LDLALQCAPD HPWAREHPEW
FTTLPDGSIA YAENPPKKYQ DIYPLNFDND PAGLYDEVLR VVRHWIDHGV KVFRVDNPHT
KPPDFWAWLI GEVKAADPDV IFLSEAFTPP ARQYGLAKLG FTQSYTYFTW RTSKWELTEF
GNEIAELADF RRPNLFVNTP DILHAVLQHN GPGMFAIRAV LAATMGPSWG MYSGYELFEH
RAVREGSEEY LDSEKYQLRP RDFAGALAEG RSLEPFIKRL NEIRRLHPAL RELRTIHFHH
VDNDALLAYS KFDPTTGDCV LVVVTLNAFA PEEATLWLDM PALGMEPYER FWVRDEITGE
EYQWGAANYV RIDPAKAVAH IINMPLIPDE SRMTLLRRR
//
