Tag | Content |
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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 |
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490 | RAFFHLLKGASPEEL | acetylation | [1] |
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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. |
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