NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1054475366|ref|WP_066274549|]
View 

L-rhamnose mutarotase [Frondihabitans sp. PAMC 28766]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
3-105 6.99e-38

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


:

Pssm-ID: 442485  Cd Length: 104  Bit Score: 123.35  E-value: 6.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFLRPDgLLIGYYETDDAIVGDRYLAASTVAAEWEAYMGQ 82
Cdd:COG3254     2 RYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN-LLFGYMEVDDFEAAMAALAADPVNQRWWALMAD 80

                          90       100
                  ....*....|....*....|....
gi 1054475366  83 IFDGIDGR-ADQVSVELEEVFNLE 105
Cdd:COG3254    81 IQETLPDAkPSEKWVPLEEVFHLD 104
 
Name Accession Description Interval E-value
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
3-105 6.99e-38

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 123.35  E-value: 6.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFLRPDgLLIGYYETDDAIVGDRYLAASTVAAEWEAYMGQ 82
Cdd:COG3254     2 RYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN-LLFGYMEVDDFEAAMAALAADPVNQRWWALMAD 80

                          90       100
                  ....*....|....*....|....
gi 1054475366  83 IFDGIDGR-ADQVSVELEEVFNLE 105
Cdd:COG3254    81 IQETLPDAkPSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-102 1.17e-32

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: 109.90  E-value: 1.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFLRPDGLLIGYYETDDAIVGDRYLAASTVAAEWEAYMGQ 82
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLREGNRLFMYMETGDDAADAALAAANPVVQEWWALMAD 80

                          90       100
                  ....*....|....*....|
gi 1054475366  83 IFDGIDGrADQVSVELEEVF 102
Cdd:pfam05336  81 FQEANPD-ASPGEKPLEEVF 99
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-105 4.74e-16

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: 67.92  E-value: 4.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFL-RPDGLLIGYYETDDAivgDRY--LAASTVAAEWEAY 79
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLdKQRNLLFAYVEIEDE---ERWnaIAETDICQKWWKY 77

                          90       100
                  ....*....|....*....|....*.
gi 1054475366  80 MGQIFDGiDGRADQVSVELEEVFNLE 105
Cdd:TIGR02625  78 MADVMPS-NPDNSPVSTDLQEVFYLD 102
 
Name Accession Description Interval E-value
RhaM COG3254
L-rhamnose mutarotase [Cell wall/membrane/envelope biogenesis];
3-105 6.99e-38

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


Pssm-ID: 442485  Cd Length: 104  Bit Score: 123.35  E-value: 6.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFLRPDgLLIGYYETDDAIVGDRYLAASTVAAEWEAYMGQ 82
Cdd:COG3254     2 RYAFVMDLKPGLIAEYKRRHAAIWPELLAALKEAGIRNYSIFLDGN-LLFGYMEVDDFEAAMAALAADPVNQRWWALMAD 80

                          90       100
                  ....*....|....*....|....
gi 1054475366  83 IFDGIDGR-ADQVSVELEEVFNLE 105
Cdd:COG3254    81 IQETLPDAkPSEKWVPLEEVFHLD 104
rhaM pfam05336
L-rhamnose mutarotase; This family contains L-rhamnose mutarotase which is a glycosyl ...
 3-102 1.17e-32

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: 109.90  E-value: 1.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFLRPDGLLIGYYETDDAIVGDRYLAASTVAAEWEAYMGQ 82
Cdd:pfam05336   1 RYAFTLDLKPELIEEYKRRHAEVWPEVLAALREAGIRNYSIFLREGNRLFMYMETGDDAADAALAAANPVVQEWWALMAD 80

                          90       100
                  ....*....|....*....|
gi 1054475366  83 IFDGIDGrADQVSVELEEVF 102
Cdd:pfam05336  81 FQEANPD-ASPGEKPLEEVF 99
YiiL_rotase TIGR02625
L-rhamnose mutarotase; Members of this protein family are rhamnose mutarotase from Escherichia ...
 3-105 4.74e-16

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: 67.92  E-value: 4.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054475366   3 RVCFQLQVDPSKLDEYRARHRAVWPSMLQEIAASGRRNYSLFL-RPDGLLIGYYETDDAivgDRY--LAASTVAAEWEAY 79
Cdd:TIGR02625   1 RKAFVMYVNPDAHEEYQKRHNEIWPELKEVLKSHGAHNYSIFLdKQRNLLFAYVEIEDE---ERWnaIAETDICQKWWKY 77

                          90       100
                  ....*....|....*....|....*.
gi 1054475366  80 MGQIFDGiDGRADQVSVELEEVFNLE 105
Cdd:TIGR02625  78 MADVMPS-NPDNSPVSTDLQEVFYLD 102
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH