ID GLGE_BIFLB Reviewed; 731 AA.
AC C6A9K7;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Balac_1458;
OS Bifidobacterium animalis subsp. lactis (strain Bl-04 / DGCC2908 / RB 4825 /
OS SD5219).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=580050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bl-04 / DGCC2908 / RB 4825 / SD5219;
RX PubMed=19376856; DOI=10.1128/jb.00155-09;
RA Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA Roberts R.F.;
RT "Comparison of the complete genome sequences of Bifidobacterium animalis
RT subsp. lactis DSM 10140 and Bl-04.";
RL J. Bacteriol. 191:4144-4151(2009).
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; CP001515; ACS46805.1; -; Genomic_DNA.
DR RefSeq; WP_004219141.1; NC_012814.1.
DR AlphaFoldDB; C6A9K7; -.
DR SMR; C6A9K7; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 66533787; -.
DR KEGG; blc:Balac_1458; -.
DR PATRIC; fig|442563.4.peg.682; -.
DR HOGENOM; CLU_015798_0_0_11; -.
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; 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; Glycosyltransferase; Transferase.
FT CHAIN 1..731
FT /note="Alpha-1,4-glucan:maltose-1-phosphate
FT maltosyltransferase"
FT /id="PRO_0000413891"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT ACT_SITE 480
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 321
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 381
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 416
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 452
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT BINDING 590..591
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT SITE 537
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
SQ SEQUENCE 731 AA; 81693 MW; 63DF2BAF6A2C082A CRC64;
MEAQHNETEA AGKPAAKKTT RTRKPRASKQ ATFIAEAPAM PIAIKEPGQF GRVNILNCQP
SVEDDVYAAR VEIGEQFTVS AQVFMEGRTK VGATAVLKNP RGRIMARVPM TVENAGLDLY
TAKLQAGEHS TLNPWDAEFA EVKKQLGNWR VAIEGWEDTY GAWLHDARIK VDVLSDVENT
LTSGSELLTR WASTRDANLN AEQRKTLREA AKSMMDTSLD AKSRLTFADN ADIEALHETN
PLRDGLTSSG DHVFHVERPK SSFSAWYQFF PRSEGAYLDD NGKKVQGNFH TAVSGLERAK
AEGFNIVYLP PIFPIGVTNR KGPDGALNAG PDDPGSPFGI GSELGGHDTV DPLLGTMDDF
KAFCQRAHEL NLEVALDFAL QCSPDHPWVK EHPNWFRTKP DGSIAYAENP PKKYQDIYPI
DFDNDLEGIE REVERIMNLW IDAGVTIFRV DNPHTKPVRF WQDVIAAVTK KHPEVLFLAE
AFTRPAMVRA LSYAGFTQSH CYFPWRNTKP QLEEFLQETN GKGGYYQHNT FWPTTPDILT
AYVRDGGVAA HAIRAVLAAL GSPSWGIYNG YELIENRQRA DAEEQSSNEK FEIKVRDWSA
ANRIGISKLL TSLNEIRSKH AATTSYHNLT ILPSANENII AFARQTEGRF TKDGRTDTLI
VVVNLDPYNE QQSSIHVDAK ALGLPTEHPY RVKDQLTGRE YDWSWDNFVS LAPWADVAHV
FHVETGEQPL D
//
