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Conserved domains on  [gi|499558379|ref|WP_011239162|]
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UDP-N-acetylglucosamine 2-epimerase [Aromatoleum aromaticum]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WecB super family cl46823
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
30-94 6.08e-17

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG0381:

Pssm-ID: 481163  Cd Length: 366  Bit Score: 74.33  E-value: 6.08e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499558379  30 FLNsaAGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLAV-IPAKRRKIPIFHMEAGTR 94
Cdd:COG0381   61 DLG--IGSGSLAEQTARILEGLE-EVLEEEKPDAVLVHGDTNSTLAAaLAAFKLGIPVAHVEAGLR 123
 
Name Accession Description Interval E-value
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
30-94 6.08e-17

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 74.33  E-value: 6.08e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499558379  30 FLNsaAGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLAV-IPAKRRKIPIFHMEAGTR 94
Cdd:COG0381   61 DLG--IGSGSLAEQTARILEGLE-EVLEEEKPDAVLVHGDTNSTLAAaLAAFKLGIPVAHVEAGLR 123
Epimerase_2 pfam02350
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ...
26-104 1.99e-15

UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.


Pssm-ID: 426733 [Multi-domain]  Cd Length: 336  Bit Score: 69.87  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499558379   26 DPEGFLNSaaGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLA-VIPAKRRKIPIFHMEAGTRLAERCLGLFE 104
Cdd:pfam02350  35 KPDYLLNS--DSQSLAKSTGLILIGLE-DVLAEEKPDLVLVLGDTNETLAgALAAFYLRIPVAHVEAGLRSFDLTEPMPE 111
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
25-94 2.30e-14

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 66.85  E-value: 2.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499558379  25 LDPEGFLNSAAGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLAVIPAKR-RKIPIFHMEAGTR 94
Cdd:cd03786   54 IKPDYDLDLMGDNQTLGAKTGGLLIGLE-EVLFEEKPDAVLVLGDTNTTLAGALAAFkLGIPVAHVEAGLR 123
 
Name Accession Description Interval E-value
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
30-94 6.08e-17

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 74.33  E-value: 6.08e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499558379  30 FLNsaAGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLAV-IPAKRRKIPIFHMEAGTR 94
Cdd:COG0381   61 DLG--IGSGSLAEQTARILEGLE-EVLEEEKPDAVLVHGDTNSTLAAaLAAFKLGIPVAHVEAGLR 123
Epimerase_2 pfam02350
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ...
26-104 1.99e-15

UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.


Pssm-ID: 426733 [Multi-domain]  Cd Length: 336  Bit Score: 69.87  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499558379   26 DPEGFLNSaaGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLA-VIPAKRRKIPIFHMEAGTRLAERCLGLFE 104
Cdd:pfam02350  35 KPDYLLNS--DSQSLAKSTGLILIGLE-DVLAEEKPDLVLVLGDTNETLAgALAAFYLRIPVAHVEAGLRSFDLTEPMPE 111
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
25-94 2.30e-14

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 66.85  E-value: 2.30e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499558379  25 LDPEGFLNSAAGSSGAAHTIGNLIIGVDhQVLVEVLPEAMLVLGDTNSCLAVIPAKR-RKIPIFHMEAGTR 94
Cdd:cd03786   54 IKPDYDLDLMGDNQTLGAKTGGLLIGLE-EVLFEEKPDAVLVLGDTNTTLAGALAAFkLGIPVAHVEAGLR 123
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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