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Conserved domains on  [gi|1444898112|gb|AXL49350|]
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L-rhamnose mutarotase [Paraburkholderia caffeinilytica]

Protein Classification

L-rhamnose mutarotase( domain architecture ID 10007127)

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
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-103 9.43e-41

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


:

Pssm-ID: 442485  Cd Length: 104  Bit Score: 130.28  E-value: 9.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   2 ETIAFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDAEshHLFAILTRTT-NHTMNALPQLDVMRKWWVYM 80
Cdd:COG3254     1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN--LLFGYMEVDDfEAAMAALAADPVNQRWWALM 78
                          90       100
                  ....*....|....*....|....*
gi 1444898112  81 ADIMQTAPDHT--PLQQPLEPLFHL 103
Cdd:COG3254    79 ADIQETLPDAKpsEKWVPLEEVFHL 103
 
Name Accession Description Interval E-value
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-103 9.43e-41

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 130.28  E-value: 9.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   2 ETIAFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDAEshHLFAILTRTT-NHTMNALPQLDVMRKWWVYM 80
Cdd:COG3254     1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN--LLFGYMEVDDfEAAMAALAADPVNQRWWALM 78
                          90       100
                  ....*....|....*....|....*
gi 1444898112  81 ADIMQTAPDHT--PLQQPLEPLFHL 103
Cdd:COG3254    79 ADIQETLPDAKpsEKWVPLEEVFHL 103
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
4-102 4.64e-38

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: 123.38  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   4 IAFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDaESHHLFAILTRTTNHTMNALPQLD-VMRKWWVYMAD 82
Cdd:pfam05336   2 YAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALAAANpVVQEWWALMAD 80
                          90       100
                  ....*....|....*....|
gi 1444898112  83 IMQTAPDHTPLQQPLEPLFH 102
Cdd:pfam05336  81 FQEANPDASPGEKPLEEVFH 100
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
5-103 6.01e-30

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: 102.98  E-value: 6.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   5 AFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDAESHHLFAILTRTTNHTMNALPQLDVMRKWWVYMADIM 84
Cdd:TIGR02625   3 AFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMADVM 82
                          90
                  ....*....|....*....
gi 1444898112  85 QTAPDHTPLQQPLEPLFHL 103
Cdd:TIGR02625  83 PSNPDNSPVSTDLQEVFYL 101
 
Name Accession Description Interval E-value
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
2-103 9.43e-41

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 130.28  E-value: 9.43e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   2 ETIAFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDAEshHLFAILTRTT-NHTMNALPQLDVMRKWWVYM 80
Cdd:COG3254     1 KRYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN--LLFGYMEVDDfEAAMAALAADPVNQRWWALM 78
                          90       100
                  ....*....|....*....|....*
gi 1444898112  81 ADIMQTAPDHT--PLQQPLEPLFHL 103
Cdd:COG3254    79 ADIQETLPDAKpsEKWVPLEEVFHL 103
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
4-102 4.64e-38

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: 123.38  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   4 IAFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDaESHHLFAILTRTTNHTMNALPQLD-VMRKWWVYMAD 82
Cdd:pfam05336   2 YAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLR-EGNRLFMYMETGDDAADAALAAANpVVQEWWALMAD 80
                          90       100
                  ....*....|....*....|
gi 1444898112  83 IMQTAPDHTPLQQPLEPLFH 102
Cdd:pfam05336  81 FQEANPDASPGEKPLEEVFH 100
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
5-103 6.01e-30

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: 102.98  E-value: 6.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1444898112   5 AFRMVLNPGMREEYERRHAQIWPELVDALHNAGVRDYRIYFDAESHHLFAILTRTTNHTMNALPQLDVMRKWWVYMADIM 84
Cdd:TIGR02625   3 AFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLDKQRNLLFAYVEIEDEERWNAIAETDICQKWWKYMADVM 82
                          90
                  ....*....|....*....
gi 1444898112  85 QTAPDHTPLQQPLEPLFHL 103
Cdd:TIGR02625  83 PSNPDNSPVSTDLQEVFYL 101
 
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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