ID   GLGE_CERSP              Reviewed;         594 AA.
AC   Q9JN46;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   03-AUG-2022, entry version 82.
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};
DE   Flags: Fragment;
GN   Name=glgE {ECO:0000255|HAMAP-Rule:MF_02124}; Synonyms=aam1;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WS8N;
RX   PubMed=10970853; DOI=10.1093/emboj/19.17.4601;
RA   Shah D.S.H., Porter S.L., Martin A.C., Hamblin P.A., Armitage J.P.;
RT   "Fine tuning bacterial chemotaxis: analysis of Rhodobacter sphaeroides
RT   behaviour under aerobic and anaerobic conditions by mutation of the major
RT   chemotaxis operons and cheY genes.";
RL   EMBO J. 19:4601-4613(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB87126.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X80205; CAB87126.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9JN46; -.
DR   SMR; Q9JN46; -.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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; Transferase.
FT   CHAIN           1..>594
FT                   /note="Alpha-1,4-glucan:maltose-1-phosphate
FT                   maltosyltransferase"
FT                   /id="PRO_0000054351"
FT   REGION          244..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        377
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   ACT_SITE        406
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   BINDING         246
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   BINDING         306
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   BINDING         341
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   BINDING         378
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   BINDING         517..518
FT                   /ligand="alpha-maltose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:63576"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   SITE            464
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02124"
FT   NON_TER         594
SQ   SEQUENCE   594 AA;  68156 MW;  6AAD0884134C08FC CRC64;
     MRLADARVAI EGVNLEIDGG RFAAKVVAGW EVAVEADIFC DGHDSIDAAV LHRQRGTDDW
     TEVRMEFLVN DRWQARVTFA ENAFHELTFL AWRDLYTTWR KEVAKKLAAG QKIDLELEEG
     RRLLQSVETA GAEDRALVDR ILGEDGADQE AGARFARMSS PEAVAAMKRC APRTNLTCYK
     ILPIFADREA AAFSAWYEMM PRSQSGDPER HGTFDDVIRK LPYVRDLGFD VLYFTPIHPI
     GRVNRKGRNN SLTPGPDDPG SPYAIGSEEG GHDAIHPELG DFESFGRLVE AAHAHGLEVA
     LDFAIQCAPD HPWIREHPEW FDWRPDGTIK FAENPPKKYE DIVNVHFYRG ALPELWYALR
     DVVLFWVEKG VKIFRVDNPH TKPFPFWEWM IGEVQSQHPD VIFLAEAFTR PKVMKRLGKV
     GYGQSYSYFT WRNTKAELID YLTELTTEEC RHYMRPNFFA NTPDINPVYL QHSGRAGFRV
     RLALAATLGG NYGLYNGYEI CEATPVPGKE EYFNSEKYQL RAWDFDQPGH IQDDIRLMNH
     IRRTHPAMRD FTRLRFYDAH NDSVLAYGKS TEDKQDFLLF HVNLDPHAAQ TFEF