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Conserved domains on  [gi|505382823|ref|WP_015569925|]
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MULTISPECIES: L-rhamnose mutarotase [Enterobacter]

Protein Classification

L-rhamnose mutarotase( domain architecture ID 10021190)

L-rhamnose mutarotase, a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-104 5.58e-68

L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia coli, previously designated YiiL as an uncharacterized protein, and close homologs also associated with rhamnose dissimilation operons in other bacterial genomes. Mutarotase is a term for an epimerase that changes optical activity. This enzyme was shown experimentally to interconvert alpha and beta stereoisomers of the pyranose form of L-rhamnose. The crystal structure of this small (104 amino acid) protein shows a locally asymmetric dimer with active site residues of His, Tyr, and Trp. [Energy metabolism, Sugars]


:

Pssm-ID: 131674  Cd Length: 102  Bit Score: 198.89  E-value: 5.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823    3 RKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDKARNLLFATVEIESEERWNAVANTDVCQRWWKYMGD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|..
gi 505382823   83 VMPSNPDNSPVSSALKEVFYLD 104
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYLD 102
 
Name Accession Description Interval E-value
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-104 5.58e-68

L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia coli, previously designated YiiL as an uncharacterized protein, and close homologs also associated with rhamnose dissimilation operons in other bacterial genomes. Mutarotase is a term for an epimerase that changes optical activity. This enzyme was shown experimentally to interconvert alpha and beta stereoisomers of the pyranose form of L-rhamnose. The crystal structure of this small (104 amino acid) protein shows a locally asymmetric dimer with active site residues of His, Tyr, and Trp. [Energy metabolism, Sugars]


Pssm-ID: 131674  Cd Length: 102  Bit Score: 198.89  E-value: 5.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823    3 RKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDKARNLLFATVEIESEERWNAVANTDVCQRWWKYMGD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|..
gi 505382823   83 VMPSNPDNSPVSSALKEVFYLD 104
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYLD 102
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-104 2.65e-42

L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442485  Cd Length: 104  Bit Score: 133.75  E-value: 2.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823   2 IRKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDKarNLLFATVEIES-EERWNAVANTDVCQRWWKYM 80
Cdd:COG3254    1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDG--NLLFGYMEVDDfEAAMAALAADPVNQRWWALM 78

                         90       100
                 ....*....|....*....|....*.
gi 505382823  81 GDVMPSNPDN--SPVSSALKEVFYLD 104
Cdd:COG3254   79 ADIQETLPDAkpSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-102 1.56e-39

L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.


Pssm-ID: 428428  Cd Length: 100  Bit Score: 126.85  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823    3 RKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDkARNLLFATVEIESEERWNAV-ANTDVCQRWWKYMG 81
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALaAANPVVQEWWALMA 79

                          90       100
                  ....*....|....*....|.
gi 505382823   82 DVMPSNPDNSPVSSALKEVFY 102
Cdd:pfam05336  80 DFQEANPDASPGEKPLEEVFH 100
 
Name Accession Description Interval E-value
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-104 5.58e-68

L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia coli, previously designated YiiL as an uncharacterized protein, and close homologs also associated with rhamnose dissimilation operons in other bacterial genomes. Mutarotase is a term for an epimerase that changes optical activity. This enzyme was shown experimentally to interconvert alpha and beta stereoisomers of the pyranose form of L-rhamnose. The crystal structure of this small (104 amino acid) protein shows a locally asymmetric dimer with active site residues of His, Tyr, and Trp. [Energy metabolism, Sugars]


Pssm-ID: 131674  Cd Length: 102  Bit Score: 198.89  E-value: 5.58e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823    3 RKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDKARNLLFATVEIESEERWNAVANTDVCQRWWKYMGD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|..
gi 505382823   83 VMPSNPDNSPVSSALKEVFYLD 104
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYLD 102
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-104 2.65e-42

L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442485  Cd Length: 104  Bit Score: 133.75  E-value: 2.65e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823   2 IRKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDKarNLLFATVEIES-EERWNAVANTDVCQRWWKYM 80
Cdd:COG3254    1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDG--NLLFGYMEVDDfEAAMAALAADPVNQRWWALM 78

                         90       100
                 ....*....|....*....|....*.
gi 505382823  81 GDVMPSNPDN--SPVSSALKEVFYLD 104
Cdd:COG3254   79 ADIQETLPDAkpSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-102 1.56e-39

L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.


Pssm-ID: 428428  Cd Length: 100  Bit Score: 126.85  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505382823    3 RKAFVMQVNPDAHEEYARRHNPIWPELEAVLKAHGAHHYAIYLDkARNLLFATVEIESEERWNAV-ANTDVCQRWWKYMG 81
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALaAANPVVQEWWALMA 79

                          90       100
                  ....*....|....*....|.
gi 505382823   82 DVMPSNPDNSPVSSALKEVFY 102
Cdd:pfam05336  80 DFQEANPDASPGEKPLEEVFH 100
 
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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