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ID Q47SE4_THEFY Unreviewed; 655 AA.
AC Q47SE4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 08-MAY-2019, entry version 94.
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 OrderedLocusNames=Tfu_0585 {ECO:0000313|EMBL:AAZ54623.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54623.1, ECO:0000313|Proteomes:UP000000434};
RN [1] {ECO:0000313|Proteomes:UP000000434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX PubMed=17209016; DOI=10.1128/JB.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA Richardson P., Wilson D.B., Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
CC -!- FUNCTION: Maltosyltransferase that uses maltose 1-phosphate (M1P)
CC as the sugar donor to elongate linear or branched alpha-(1->4)-
CC glucans. Is involved in a branched alpha-glucan biosynthetic
CC pathway from trehalose, together with TreS, Mak and GlgB.
CC {ECO:0000256|HAMAP-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;
CC Xref=Rhea:RHEA:42692, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:10183,
CC ChEBI:CHEBI:15444, ChEBI:CHEBI:43474, ChEBI:CHEBI:63576;
CC EC=2.4.99.16; Evidence={ECO:0000256|HAMAP-Rule:MF_02124};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02124}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgE
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02124}.
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DR EMBL; CP000088; AAZ54623.1; -; Genomic_DNA.
DR RefSeq; WP_011291032.1; NC_007333.1.
DR STRING; 269800.Tfu_0585; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAZ54623; AAZ54623; Tfu_0585.
DR KEGG; tfu:Tfu_0585; -.
DR eggNOG; ENOG4105EP6; Bacteria.
DR eggNOG; COG0366; LUCA.
DR HOGENOM; HOG000239230; -.
DR KO; K16147; -.
DR OMA; RPNFWPN; -.
DR OrthoDB; 1573900at2; -.
DR BioCyc; TFUS269800:G1G4Q-595-MONOMER; -.
DR Proteomes; UP000000434; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:UniProtKB-UniRule.
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;
DR PRODOM; Q47SE4.
DR SWISS-2DPAGE; Q47SE4.
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02124};
KW Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_02124};
KW Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02124}.
FT DOMAIN 191 548 Aamy. {ECO:0000259|SMART:SM00642}.
FT REGION 519 520 Maltose 1-phosphate binding.
FT {ECO:0000256|HAMAP-Rule:MF_02124}.
FT ACT_SITE 379 379 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_02124}.
FT ACT_SITE 408 408 Proton donor. {ECO:0000256|HAMAP-Rule:
FT MF_02124}.
FT BINDING 249 249 Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT Rule:MF_02124}.
FT BINDING 309 309 Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT Rule:MF_02124}.
FT BINDING 344 344 Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT Rule:MF_02124}.
FT BINDING 380 380 Maltose 1-phosphate. {ECO:0000256|HAMAP-
FT Rule:MF_02124}.
FT SITE 465 465 Transition state stabilizer.
FT {ECO:0000256|HAMAP-Rule:MF_02124}.
SQ SEQUENCE 655 AA; 73698 MW; BB2ED2A48C836616 CRC64;
MIGRFPILDV SPVVDIGTAK AVVGETFPVR ATVFREGHEA LGAGVVLYTP EGQRQPLVPL
REIAPGTDRY EAEVTVTSEG LWHFAIEAWS DPYATWCHDA RIKIPAGQDV ELMLEEGARL
LERAARRVPR RPALAEIAAA MRDGSRSAHE RLDLALSDLV RDELAERPLR ELVTRSQRFP
VMVSRRRALF GSWYEFFPRS EGAVLDTEDG EPRSGTFATA ARRLPAIADM GFDVVYIPPI
HPVGYSFRKG RNNSTVAQPG DPGSVWAIGS HEGGHDAIHP DLGTIDDFDA FVARARELGL
EIAMDLALQA SPDHPWVKEH PEWFTVRADG SIAYAENPPK KYQDIYPINF DKDPEGIFTE
VRRIVRYWMS HGVRIFRVDN PHTKPVAFWE RLLADIAATD PDVIFLSEAF TRPAMMHTLA
KIGFHQSYTY FTWRNTKQEL EEYLTELTGE AAAYMRPNFF VNTPDILHAY LQHGGRPAFE
VRAILAATLS PTWGMYSGYE LCENRALKPG SEEYLDSEKY QYKPRDWEAA EAAGITITPL
IRKLNSLRRS HPALQELRNL RFHYADQPEI ICYSKRLAGA NHGADDTILV VANLDPHHTR
EATVWLDMPA LGFAPGDHIT VTDQLSGHSY HWVEANYVRL DPHVQTAHIF TVAPA
//
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