CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013869
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 1,4-alpha-glucan branching enzyme TTHA1902 
Protein Synonyms/Alias
 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase; Alpha-(1->4)-glucan branching enzyme; Branching enzyme; BE 
Gene Name
 TTHA1902; TT1467 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) 
NCBI Taxa ID
 300852 
Lysine Modification
Position
Peptide
Type
References
490RAFFHLLKGASPEELacetylation[1]
Reference
 [1] Acetylome with structural mapping reveals the significance of lysine acetylation in Thermus thermophilus.
 Okanishi H, Kim K, Masui R, Kuramitsu S.
 J Proteome Res. 2013 Aug 1;. [PMID: 23901841
Functional Description
 Catalyzes the formation of branch points in alpha- glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha- 1,4-linked oligosaccharides of 2-7 glucose residues, beta- cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl- beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin). 
Sequence Annotation
 ACT_SITE 184 184 Nucleophile.
 ACT_SITE 353 353 Proton donor.
 BINDING 265 265 Substrate (By similarity).
 BINDING 282 282 Substrate; via amide nitrogen (By
 BINDING 404 404 Substrate (By similarity).
 BINDING 460 460 Substrate (By similarity).
 BINDING 469 469 Substrate (By similarity).  
Keyword
 3D-structure; Carbohydrate metabolism; Complete proteome; Glycogen biosynthesis; Glycogen metabolism; Glycosyltransferase; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 520 AA 
Protein Sequence
MARFALVLHA HLPYVRAHGM WPFGEETLYE AMAETYLPLI RVLERLRAEG VEAPFTLGIT 60
PILAEQLADA RIKEGFWAYA KDRLERAQGD YQRYRGTALE ASARHQVAFW ELTLDHFQRL 120
SGDLVAAFRK AEEGGQVELI TSNATHGYSP LLGYDEALWA QIKTGVSTYR RHFAKDPTGF 180
WLPEMAYRPK GPWKPPVEGP PEGVRPGVDE LLMRAGIRYT FVDAHLVQGG EPLSPYGEAA 240
LGPVESQEAT YHVHELESGL RVLARNPETT LQVWSADYGY PGEGLYREFH RKDPLSGLHH 300
WRVTHRKADL AEKAPYDPEA AFAKTEEHAR HFVGLLERLA GRHPEGVILS PYDAELFGHW 360
WYEGVAWLEA VLRLLAQNPK VRPVTAREAV QGPAVRTALP EGSWGRGGDH RVWLNEKTLD 420
YWEKVYRAEG AMREAARRGV LPEGVLRQAM RELLLLEASD WPFLMETGQA EAYARERYEE 480
HARAFFHLLK GASPEELRAL EERDNPFPEA DPRLYLFREA 520 
Gene Ontology
 GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IDA:UniProtKB.
 GO:0005978; P:glycogen biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR015293; DUF1957.
 IPR011330; Glyco_hydro/deAcase_b/a-brl.
 IPR027291; Glyco_hydro_38/57_N.
 IPR004300; Glyco_hydro_57_N. 
Pfam
 PF09210; DUF1957
 PF03065; Glyco_hydro_57 
SMART
  
PROSITE
  
PRINTS