1FDY
N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | d1fdya_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Aldolase | Class I aldolase | N-acetylneuraminate lyase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
B | d1fdyb_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Aldolase | Class I aldolase | N-acetylneuraminate lyase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
C | d1fdyc_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Aldolase | Class I aldolase | N-acetylneuraminate lyase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
D | d1fdyd_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Aldolase | Class I aldolase | N-acetylneuraminate lyase | (Escherichia coli ) [TaxId: 562 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | Aldolase | 8044525 | 3000445 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Aldolase | 8044525 | 3000445 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Aldolase | 8044525 | 3000445 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Aldolase | 8044525 | 3000445 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | DHDPS | e1fdyA1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHDPS | ECOD (1.6) |
B | DHDPS | e1fdyB1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHDPS | ECOD (1.6) |
C | DHDPS | e1fdyC1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHDPS | ECOD (1.6) |
D | DHDPS | e1fdyD1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: DHDPS | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.20.20.70 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Aldolase class I | CATH (4.3.0) |
B | 3.20.20.70 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Aldolase class I | CATH (4.3.0) |
C | 3.20.20.70 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Aldolase class I | CATH (4.3.0) |
D | 3.20.20.70 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Aldolase class I | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR005264 | N-acetylneuraminate lyase | Family | |
IPR020624 | Schiff base-forming aldolase, conserved site | Conserved Site | |
IPR013785 | Aldolase-type TIM barrel | Homologous Superfamily | |
IPR020625 | Schiff base-forming aldolase, active site | Active Site | |
IPR002220 | DapA-like | Family |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic Residues |
---|---|---|---|
N-acetylneuraminate lyase M-CSA #553 | The N-acetylneuraminate lyase (NAL) enzymes are a subfamily of the (beta/alpha)8 enzymes. They all share a common catalytic step but catalyse reactions in different biological pathways. The formation of a Schiff base between a strictly conserved lysine residue and the C2 carbon of the common keto-acid moiety of the substrate is a common feature of the group, with the NAL enzymes catalysing the aldol cleavage of N-acetylneuraminate to form N-acetylmannosine and pyruvate via the distinctive Schiff base intermediate. | EC: 4.1.3.3 (PDB Primary Data) |