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Conserved domains on  [gi|1391268174|ref|WP_109408571|]
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MULTISPECIES: L-rhamnose mutarotase [Proteus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rhaM super family cl01281
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-103 5.10e-61

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.


The actual alignment was detected with superfamily member TIGR02625:

Pssm-ID: 470145  Cd Length: 102  Bit Score: 181.17  E-value: 5.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   3 RKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDKKRNLLFGYVQIESEVQWNAVANTEICQKWWKYMSD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|.
gi 1391268174  83 VMPSNPDNSPISDNLHEVFFL 103
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYL 101
 
Name Accession Description Interval E-value
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-103 5.10e-61

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: 181.17  E-value: 5.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   3 RKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDKKRNLLFGYVQIESEVQWNAVANTEICQKWWKYMSD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|.
gi 1391268174  83 VMPSNPDNSPISDNLHEVFFL 103
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYL 101
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-104 5.10e-39

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 125.66  E-value: 5.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   2 IRKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDKkrNLLFGYVQIES-EVQWNAVANTEICQKWWKYM 80
Cdd:COG3254     1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDG--NLLFGYMEVDDfEAAMAALAADPVNQRWWALM 78

                          90       100
                  ....*....|....*....|....*.
gi 1391268174  81 SDVMPSNPDN--SPISDNLHEVFFLK 104
Cdd:COG3254    79 ADIQETLPDAkpSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-101 1.45e-35

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: 116.83  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   3 RKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDkKRNLLFGYVQIESEVQWNAV-ANTEICQKWWKYMS 81
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALaAANPVVQEWWALMA 79

                          90       100
                  ....*....|....*....|
gi 1391268174  82 DVMPSNPDNSPISDNLHEVF 101
Cdd:pfam05336  80 DFQEANPDASPGEKPLEEVF 99
 
Name Accession Description Interval E-value
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-103 5.10e-61

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: 181.17  E-value: 5.10e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   3 RKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDKKRNLLFGYVQIESEVQWNAVANTEICQKWWKYMSD 82
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMAD 80

                          90       100
                  ....*....|....*....|.
gi 1391268174  83 VMPSNPDNSPISDNLHEVFFL 103
Cdd:TIGR02625  81 VMPSNPDNSPVSTDLQEVFYL 101
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-104 5.10e-39

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 125.66  E-value: 5.10e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   2 IRKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDKkrNLLFGYVQIES-EVQWNAVANTEICQKWWKYM 80
Cdd:COG3254     1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDG--NLLFGYMEVDDfEAAMAALAADPVNQRWWALM 78

                          90       100
                  ....*....|....*....|....*.
gi 1391268174  81 SDVMPSNPDN--SPISDNLHEVFFLK 104
Cdd:COG3254    79 ADIQETLPDAkpSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-101 1.45e-35

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: 116.83  E-value: 1.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391268174   3 RKAFVMQVNANSHQEYQQRHNPIWQELEATLKAHGAHNYSIFLDkKRNLLFGYVQIESEVQWNAV-ANTEICQKWWKYMS 81
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALaAANPVVQEWWALMA 79

                          90       100
                  ....*....|....*....|
gi 1391268174  82 DVMPSNPDNSPISDNLHEVF 101
Cdd:pfam05336  80 DFQEANPDASPGEKPLEEVF 99
 
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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