(data stored in SCRATCH zone)

SWISSPROT: Q47SE4_THEFY

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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