Tag | Content |
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CPLM ID | CPLM-002539 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Fructose-bisphosphate aldolase |
Protein Synonyms/Alias | |
Gene Name | Ald |
Gene Synonyms/Alias | CG6058 |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
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42 | ESGPTMGKRLQDIGV | acetylation | [1] | 230 | YLEGTLLKPNMVTAG | acetylation | [1] |
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Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | May take part in developmental stage-specific or tissue -specific sugar-phosphate metabolisms. Protein acts on two substrates fructose 1,6-bisphosphate and fructose 1-phosphate (like other class I aldolases). |
Sequence Annotation | ACT_SITE 188 188 Proton acceptor (By similarity). ACT_SITE 230 230 Schiff-base intermediate with BINDING 56 56 Substrate. BINDING 147 147 Substrate. MOD_RES 2 2 N-acetylthreonine. |
Keyword | 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Glycolysis; Lyase; Reference proteome; Schiff base. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 361 AA |
Protein Sequence | MTTYFNYPSK ELQDELREIA QKIVAPGKGI LAADESGPTM GKRLQDIGVE NTEDNRRAYR 60 QLLFSTDPKL AENISGVILF HETLYQKADD GTPFAEILKK KGIILGIKVD KGVVPLFGSE 120 DEVTTQGLDD LAARCAQYKK DGCDFAKWRC VLKIGKNTPS YQSILENANV LARYASICQS 180 QRIVPIVEPE VLPDGDHDLD RAQKVTETVL AAVYKALSDH HVYLEGTLLK PNMVTAGQSA 240 KKNTPEEIAL ATVQALRRTV PAAVTGVTFL SGGQSEEEAT VNLSAINNVP LIRPWALTFS 300 YGRALQASVL RAWAGKKENI AAGQNELLKR AKANGDAAQG KYVAGSAGAG SGSLFVANHA 360 Y 361 |
Gene Ontology | |
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SMART | |
PROSITE | |
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