AC   MF_01237;
DC   Protein; auto
TR   HAMAP; MF_01237; -; 1; level=0
XX
Names: N_acetylneuram_lyase
XX
ID   NANA
DE   RecName: Full=N-acetylneuraminate lyase;
DE            Short=Neu5Ac lyase;
DE            Short=NAL;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE   AltName: Full=N-acetylneuraminic acid aldolase;
DE   AltName: Full=Sialate lyase;
DE   AltName: Full=Sialic acid aldolase;
DE   AltName: Full=Sialic acid lyase;
GN   Name=nanA;
XX
CC   -!- FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic
CC       acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine
CC       (ManNAc) via a Schiff base intermediate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aceneuramate = N-acetyl-D-mannosamine + pyruvate;
CC         Xref=Rhea:RHEA:23296, ChEBI:CHEBI:15361, ChEBI:CHEBI:17122,
CC         ChEBI:CHEBI:173083; EC=4.1.3.3;
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC       fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the DapA family. NanA subfamily.
XX
DR   Pfam; PF00701; DHDPS; 1; trigger=no
DR   PRINTS; PR00146; DHPICSNTHASE; 1; trigger=no
DR   NCBIfam; TIGR00683; nanA; 1; trigger=no
DR   PROSITE; PS00665; DHDPS_1; 1; trigger=no
DR   PROSITE; PS00666; DHDPS_2; 1; trigger=no
DR   PIRSF; PIRSF001365; DHDPS; 1; trigger=no
XX
KW   Cytoplasm
KW   Carbohydrate metabolism
KW   Lyase
KW   Schiff base
XX
GO   GO:0008747; F:N-acetylneuraminate lyase activity
GO   GO:0005975; P:carbohydrate metabolic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: NANA_ECOLI (P0A6L4)
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT   Condition: Y
FT   ACT_SITE        165
FT                   /note="Schiff-base intermediate with substrate"
FT   Condition: K
FT   BINDING         47
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: S
FT   BINDING         48
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: [TS]
FT   BINDING         167
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: [TS]
FT   BINDING         189
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: G
FT   BINDING         191
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: D
FT   BINDING         192
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: E
FT   BINDING         208
FT                   /ligand="aceneuramate"
FT                   /ligand_id="ChEBI:CHEBI:173083"
FT   Condition: [SG]
XX
Size: 280-320;
Related: MF_00418; MF_00694;
Template: P0A6L4; P44539; Q9S4K9; Q2G160; P59407; Q6GK01; A7B555; Q8RDN6; Q9CKB0;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in ECOL6
Plasmid: in RHIME
Comments: None
XX
# Revision 1.36 2023/12/15
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