HAMAP rule MF_01237
General rule information
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Accession | MF_01237 |
Dates | 21-MAR-2003 (Created)
2-MAY-2024 (Last updated, Version 38) |
Name | N_acetylneuram_lyase |
Scope(s) |
Bacteria |
Template(s) | P0A6L4 (NANA_ECOLI); P44539 (NANA_HAEIN); Q9S4K9 (NANA_CLOPE); Q2G160 (NANA_STAA8); P59407 (NANA_LACPL); Q6GK01 (NANA_STAAR); A7B555 (NANA_MEDG7); Q8RDN6 (NANA_FUSNN); Q9CKB0 (NANA_PASMU); [ Recover all ] |
Triggered by |
HAMAP; MF_01237 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | NANA |
Protein name | RecName: Full=N-acetylneuraminate lyase; Short=Neu5Ac lyase; Short=NAL; EC=4.1.3.3; AltName: Full=N-acetylneuraminate pyruvate-lyase; AltName: Full=N-acetylneuraminic acid aldolase; AltName: Full=Sialate lyase; AltName: Full=Sialic acid aldolase; AltName: Full=Sialic acid lyase; |
Gene name | Name=nanA; |
Comments
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FUNCTION | Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. |
CATALYTIC ACTIVITY | Reaction=aceneuramate = aldehydo-N-acetyl-D-mannosamine + pyruvate; Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122, ChEBI:CHEBI:173083; EC=4.1.3.3; |
PATHWAY | Amino-sugar metabolism; N-acetylneuraminate degradation; D- fructose 6-phosphate from N-acetylneuraminate: step 1/5. |
SUBUNIT | Homotetramer. |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the DapA family. NanA subfamily. |
Keywords
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Gene Ontology
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GO:0008747; Molecular function:N-acetylneuraminate lyase activity |
GO:0005975; Biological process:carbohydrate metabolic process |
GO:0019262; Biological process:N-acetylneuraminate catabolic process |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Pfam | PF00701; DHDPS; 1; |
PRINTS | PR00146; DHPICSNTHASE; 1; |
NCBIfam | TIGR00683; nanA; 1; |
PROSITE | PS00665; DHDPS_1; 1; |
PROSITE | PS00666; DHDPS_2; 1; |
PIRSF | PIRSF001365; DHDPS; 1; |
Features
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From: NANA_ECOLI (P0A6L4) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 137 | 137 | /note="Proton donor" | Y | ||||||||
ACT_SITE | 165 | 165 | /note="Schiff-base intermediate with substrate" | K | ||||||||
BINDING | 47 | 47 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
S | ||||||||
BINDING | 48 | 48 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
[TS] | ||||||||
BINDING | 167 | 167 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
[TS] | ||||||||
BINDING | 189 | 189 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
G | ||||||||
BINDING | 191 | 191 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
D | ||||||||
BINDING | 192 | 192 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
E | ||||||||
BINDING | 208 | 208 | /ligand="aceneuramate" /ligand_id="ChEBI:CHEBI:173083" |
[SG] |
Additional information
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Size range | 280-320 amino acids |
Related rules |
MF_00418 MF_00694 |
Fusion | Nter: None Cter: None |