Tag | Content |
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CPLM ID | CPLM-014687 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | N-acetylneuraminate lyase |
Protein Synonyms/Alias | NALase; N-acetylneuraminate pyruvate-lyase; N-acetylneuraminic acid aldolase; Sialate lyase; Sialate-pyruvate lyase; Sialic acid aldolase; Sialic acid lyase |
Gene Name | Npl |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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299 | FTANAEAKLKSLNFL | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N- glycolylneuraminic acid (Neu5Gc) degradation pathway (By similarity). |
Sequence Annotation | REGION 51 52 Substrate binding (By similarity). ACT_SITE 173 173 Schiff-base intermediate with substrate |
Keyword | Carbohydrate metabolism; Complete proteome; Cytoplasm; Lyase; Reference proteome; Schiff base. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 320 AA |
Protein Sequence | MAFPKKKLQG LVAATITPMT ENGEINFPVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSI 60 SERRQVAEEW VRQGKNKLDQ VVIHVGALNL KESQELAQHA AEIGADGIAV IAPFFFKSQN 120 KDALISFLRE VAAAAPALPF YYYHIPSLTG VKIRAEELLD GIQDKIPSFQ GLKFSDTDLL 180 DFGQCVDQNH QRQFALLFGV DEQLLSALVL GATGAVGSTY NYLGKKTNQM LEAFEQKDLA 240 SALSYQFRIQ RFINYVIKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKATQ EFTANAEAKL 300 KSLNFLSFPG LKDGNMEACS 320 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0008747; F:N-acetylneuraminate lyase activity; ISS:UniProtKB. GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. |
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PRINTS | |