N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
8-362
6.16e-146
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine.
Pssm-ID: 274655 [Multi-domain] Cd Length: 329 Bit Score: 415.83 E-value: 6.16e-146
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
29-295
9.26e-102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.
Pssm-ID: 427137 Cd Length: 239 Bit Score: 300.20 E-value: 9.26e-102
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
309-362
2.18e-13
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).
Pssm-ID: 212160 [Multi-domain] Cd Length: 58 Bit Score: 64.28 E-value: 2.18e-13
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to ...
8-362
6.16e-146
N-acetylneuraminate synthase; This family is a subset of the pfam03102 and is believed to include only authentic NeuB N-acetylneuraminate (sialic acid) synthase enzymes. The majority of the genes identified by this model are observed adjacent to both the NeuA and NeuC genes which together effect the biosynthesis of CMP-N-acetylneuraminate from UDP-N-acetylglucosamine.
Pssm-ID: 274655 [Multi-domain] Cd Length: 329 Bit Score: 415.83 E-value: 6.16e-146
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes ...
29-295
9.26e-102
NeuB family; NeuB is the prokaryotic N-acetylneuraminic acid (Neu5Ac) synthase. It catalyzes the direct formation of Neu5Ac (the most common sialic acid) by condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine (ManNAc). This reaction has only been observed in prokaryotes; eukaryotes synthesize the 9-phosphate form, Neu5Ac-9-P, and utilize ManNAc-6-P instead of ManNAc. Such eukaryotic enzymes are not present in this family. This family also contains SpsE spore coat polysaccharide biosynthesis proteins.
Pssm-ID: 427137 Cd Length: 239 Bit Score: 300.20 E-value: 9.26e-102
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 ...
9-360
1.95e-79
pseudaminic acid synthase; Members of this family are included within the larger pfam03102 (NeuB) family. NeuB itself (TIGR03569) is involved in the biosynthesis of neuraminic acid by the condensation of phosphoenolpyruvate (PEP) with N-Acetyl-D-Mannosamine. In an analagous reaction, this enzyme, PseI, condenses PEP with 6-deoxy-beta-L-AltNAc4NAc to generate pseudaminic acid.
Pssm-ID: 163337 [Multi-domain] Cd Length: 327 Bit Score: 246.45 E-value: 1.95e-79
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate ...
309-362
2.18e-13
C-terminal SAF domain of sialic acid synthetase; Sialic acid synthetase (N-acetylneuraminate synthase or N-acetylneuraminate-9-phosphate synthase) catalyzes the condensation of phosphoenolpyruvate with N-acetylmannosamine (ManNAc, in bacteria) or N-acetylmannosamine-6-phosphate (ManNAc-6P, in mammals), to yield N-acetylneuramic acid (NeuNAc) or N-acetylneuramic acid-9-phosphate (NeuNAc-9P), respectively. The N-terminal NeuB domain, a TIM-barrel-like structure, contains the catalytic site, the function of the SAF domain is not as clear. It may participate in domain-swapped dimerization and play a role in binding the substrate, in either domain-swapped dimers or by directly interacting with the N-terminal domain. Also included in the family are PEP-sugar pyruvyltransferases known as spore coat polysaccharide biosynthesis proteins (SpsE).
Pssm-ID: 212160 [Multi-domain] Cd Length: 58 Bit Score: 64.28 E-value: 2.18e-13
SAF domain; This domain family includes a range of different proteins. Such as antifreeze ...
309-362
1.50e-05
SAF domain; This domain family includes a range of different proteins. Such as antifreeze proteins and flagellar FlgA proteins, and CpaB pilus proteins.
Pssm-ID: 430140 [Multi-domain] Cd Length: 63 Bit Score: 42.16 E-value: 1.50e-05
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus ...
313-362
3.89e-03
SAF domains of the flagella basal body P-ring formation protein FlgA and the flp pilus assembly CpaB; FlgA is a putative periplasmic chaperone that assists in the formation of the flagellar P ring; CpaB is a protein invoved in the assembly of the flp pili, which are bacterial virulence factors mediating non-specific adherence to surfaces; these proteins appear to contain a single SAF domain. This intermediate family also contains the SAF domains of sialic acid synthetases and type III antifreeze proteins, which also share the same extensive core structure.
Pssm-ID: 212159 [Multi-domain] Cd Length: 61 Bit Score: 35.14 E-value: 3.89e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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