GLGE_MYXXD
ID GLGE_MYXXD Reviewed; 665 AA.
AC Q1D651;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
DE Short=GMPMT {ECO:0000255|HAMAP-Rule:MF_02124};
DE EC=2.4.99.16 {ECO:0000255|HAMAP-Rule:MF_02124};
DE AltName: Full=(1->4)-alpha-D-glucan:maltose-1-phosphate alpha-D-maltosyltransferase {ECO:0000255|HAMAP-Rule:MF_02124};
GN Name=glgE {ECO:0000255|HAMAP-Rule:MF_02124}; OrderedLocusNames=MXAN_3685;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_02124};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02124}.
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DR EMBL; CP000113; ABF91735.1; -; Genomic_DNA.
DR RefSeq; WP_011553703.1; NC_008095.1.
DR AlphaFoldDB; Q1D651; -.
DR SMR; Q1D651; -.
DR STRING; 246197.MXAN_3685; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; ABF91735; ABF91735; MXAN_3685.
DR GeneID; 41361020; -.
DR KEGG; mxa:MXAN_3685; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_015798_0_0_7; -.
DR OMA; RPNFWPN; -.
DR OrthoDB; 1573900at2; -.
DR Proteomes; UP000002402; 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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR HAMAP; MF_02124; GlgE; 1.
DR InterPro; IPR026585; GlgE.
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; PTHR10357:SF203; PTHR10357:SF203; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF11896; DUF3416; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..665
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413898"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 255
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 315
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 350
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 387
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 526..527
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 473
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 665 AA; 75924 MW; 22031F5C3402CF42 CRC64;
MTERLGSVFI EGVSPELDAG RHAVKRVVGE RCTVKADVFK EGHDVLVAVI RWRQVTPRAQ
QTDWEEVPMR FLGNDRWEGE FPLTRNGRYE YTIEAWPDLF RTWTSELKRK VDAGRDVRSE
LLEGAALLEG AVARARTAKQ PDDARVLGEA AVRLRQPPSP DLLAVALAPE LADVASTHPD
RSLARRYDKV LEVFADREKA RFSAWYEFFP RSAKRDGVTH ATFRDAEGWL PYIQQLGFDT
VYLPPIHPIG RTARKGKNNS LAAAADDVGS PWAIGASEGG HKAVHPKLGT LEDFRHFVET
AQAHGIEVAL DLAFQCSPDH PYVKEHPEWF QHRPDGTIKT AENPPKRYED IVNFDWMGPA
RESLWAELES VVLHWVKQGV NTFRVDNPHT KPTQFWAWLI RRVQEAHPQV LFLSEAFTRP
KVMKALGKVG FTQSYTYFTW RNFKGELQEY LEEITQPPVS DYFRGNLWPN TPDILPEFLQ
NAGPGAFRLR AALAGTLSSV WGMYCGYELC EGRPIPGKEE YTDSEKYQLV AWDLDRPGNI
RDWIARLNAA RRTHPALHQY GTLRFFSSNN DRVLFYGKRT PDGGSLVLMA VSLDPYAAQE
ALLHVPLEWL GARPDETYQV HELMSDQRSL WQGPDVQVRL TPEQPAALWA VHRFRRTENA
FDYYE
