ID C0W016_9ACTO Unreviewed; 707 AA.
AC C0W016;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
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=HMPREF0044_0894 {ECO:0000313|EMBL:EEH63875.1};
OS Gleimia coleocanis DSM 15436.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Gleimia.
OX NCBI_TaxID=525245 {ECO:0000313|EMBL:EEH63875.1, ECO:0000313|Proteomes:UP000010301};
RN [1] {ECO:0000313|EMBL:EEH63875.1, ECO:0000313|Proteomes:UP000010301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15436 {ECO:0000313|EMBL:EEH63875.1,
RC ECO:0000313|Proteomes:UP000010301};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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}.
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:EEH63875.1}.
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DR EMBL; ACFG01000030; EEH63875.1; -; Genomic_DNA.
DR AlphaFoldDB; C0W016; -.
DR STRING; 525245.HMPREF0044_0894; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_015798_0_0_11; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000010301; 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 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:UP000010301};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02124}.
FT DOMAIN 243..575
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 426
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT ACT_SITE 455
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 296
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 356
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 391
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 427
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT BINDING 565..566
FT /ligand="alpha-maltose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:63576"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
FT SITE 512
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02124"
SQ SEQUENCE 707 AA; 79080 MW; 6FED6E6FB2EFB984 CRC64;
MTTIKRRVTI RKTALKNQVP ELARITRIPA TEVFPVIEGG LWAAKTTEGE AFPVRATVFR
EGHDALAAEA VLLSPEGKVE QRVHMYDTDP GLDRYEAWLQ AAYPGNWTFR IDTWSDPYAT
WSHDATVKIA ADTDVELMLE EGALLFERAL RGEVFAILTE KSMKSALVKK TPELDSASIT
ILAEAISLLR DPEATPQRRL SAGLSNKVRK VFKQFPVRDL LTSTREYPLQ VDRKLALYGS
WYEIFPRSYG AVQDAEGNWI SGTLEAASLE LPRISDMGFD VIYLTPIHPI GTTHRKGKNN
TLTAGPNDPG SPYGIGAVTG GHDAVHPDLG TFEDFDAFVK TAKANGLEVA LDLALQCSPD
HPWVAEHPEW FTTRADGSIA YAENPPKKYQ DIYPLNFDND PEGIYLAIRN VVYTWIKHGV
TLFRVDNPHT KPLSFWQRLL AEVRSTHPEV IFLAEAFTKP AMMRTLGAIG FHQSYTYFTW
RTTKEQLEEY FTEVSAETAH LMRPAFWPTT HDILTPQMTA GGTAMFALRA VLAATAAPTW
GIYSGYEFVE KEPRPGYEEQ NDNEKYEYRP RDWSKVNDYG IANLLTLLNS ARANHPALQQ
LHNLTIHPTS DDRLICFSKH VDAKHSATGE ADTVIVVVNL DPENTVQGQV YLDFAKLGVA
GQHTSEGPLL SVVDQLDGRE YQWGETNFVE LCPQVRTAHV LAVKHGD
//
