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Conserved domains on  [gi|491797667|ref|WP_005605355|]
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dTDP-4-dehydrorhamnose 3,5-epimerase [Actinobacillus pleuropneumoniae]

Protein Classification

dTDP-4-dehydrorhamnose 3,5-epimerase family protein( domain architecture ID 10004867)

dTDP-4-dehydrorhamnose 3,5-epimerase family protein such as dTDP-4-keto-6-deoxy-D-glucose epimerase that converts dTDP-4-dehydro-6-deoxy-alpha-D-glucose into dTDP-4-dehydro-beta-L-rhamnose or dTDP-4-dehydro-6-deoxy-alpha-D-allose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RfbC COG1898
dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis] ...
1-176 5.43e-120

dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 441502  Cd Length: 177  Bit Score: 336.27  E-value: 5.43e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   1 MKIIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQT-ENTQGKLVRVVQGAV 79
Cdd:COG1898    1 MKVIETAIPGVLLIEPKVFGDERGFFFETFNAEEFAEAGLDFDFVQDNHSRSRKGVLRGLHFQLpPHAQAKLVRVVRGAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667  80 FDVAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDG 159
Cdd:COG1898   81 FDVAVDLRKGSPTFGQWVGVELSAENGRQLYIPEGFAHGFLTLSDDAEVLYKVTDYYAPEAERGIRWNDPDLGIDWPLPL 160
                        170
                 ....*....|....*..
gi 491797667 160 EPSLSVKDLAGKVLADA 176
Cdd:COG1898  161 EPILSEKDAAAPTLAEA 177
 
Name Accession Description Interval E-value
RfbC COG1898
dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis] ...
1-176 5.43e-120

dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441502  Cd Length: 177  Bit Score: 336.27  E-value: 5.43e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   1 MKIIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQT-ENTQGKLVRVVQGAV 79
Cdd:COG1898    1 MKVIETAIPGVLLIEPKVFGDERGFFFETFNAEEFAEAGLDFDFVQDNHSRSRKGVLRGLHFQLpPHAQAKLVRVVRGAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667  80 FDVAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDG 159
Cdd:COG1898   81 FDVAVDLRKGSPTFGQWVGVELSAENGRQLYIPEGFAHGFLTLSDDAEVLYKVTDYYAPEAERGIRWNDPDLGIDWPLPL 160
                        170
                 ....*....|....*..
gi 491797667 160 EPSLSVKDLAGKVLADA 176
Cdd:COG1898  161 EPILSEKDAAAPTLAEA 177
dTDP_sugar_isom pfam00908
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of ...
12-174 3.13e-108

dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.


Pssm-ID: 459991  Cd Length: 164  Bit Score: 305.84  E-value: 3.13e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   12 KLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQT-ENTQGKLVRVVQGAVFDVAVDLRKSS 90
Cdd:pfam00908   1 LLIEPKVFGDERGFFFESFNAEEFAAAGLDVDFVQDNHSRSKKGVLRGLHYQLpPHAQAKLVRVVRGEVFDVAVDLRKGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   91 PTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDGEPSLSVKDLAG 170
Cdd:pfam00908  81 PTFGQWVGVELSAENKRQLYIPEGFAHGFLVLSDDAEVLYKVTEYYAPEHERGIRWNDPDLGIDWPLPDEPILSEKDAAA 160

                  ....
gi 491797667  171 KVLA 174
Cdd:pfam00908 161 PLLA 164
rmlC TIGR01221
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of ...
2-176 3.36e-104

dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of dTDP-L-rhamnose, often as a precursor to LPS O-antigen [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273510  Cd Length: 176  Bit Score: 296.23  E-value: 3.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667    2 KIIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQTENTQGKLVRVVQGAVFD 81
Cdd:TIGR01221   1 NFIRTEIPDVLLIEPRVFGDERGFFMETYNDEAFQEQGIPVRFVQDNHSKSYKGVLRGLHYQRPHPQGKLVRVLRGEVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   82 VAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDGEP 161
Cdd:TIGR01221  81 VAVDLRRNSPTFGKWVGVLLSAENKRQLWIPEGFAHGFVVLSDEAEFLYKCTDYYAPEYERGIIWNDPDIGIDWPLEDAP 160
                         170
                  ....*....|....*
gi 491797667  162 SLSVKDLAGKVLADA 176
Cdd:TIGR01221 161 ILSEKDRNGPPLAEA 175
cupin_RmlC cd00438
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine ...
3-169 8.48e-104

RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380337  Cd Length: 168  Bit Score: 295.10  E-value: 8.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   3 IIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQTE-NTQGKLVRVVQGAVFD 81
Cdd:cd00438    1 FTETAIPGVLLIEPKVFGDERGFFAETFNKEEFAEAGINPDFVQDNHSFSKKGVLRGLHFQLPpHAQAKLVRCLRGAIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667  82 VAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDgEP 161
Cdd:cd00438   81 VAVDLRKGSPTFGQWVGVELSAENHRQLYIPEGFAHGFQTLSDDAEVLYKCSDYYAPESERGIRWNDPDLGIDWPLP-EP 159

                 ....*...
gi 491797667 162 SLSVKDLA 169
Cdd:cd00438  160 ILSEKDRN 167
 
Name Accession Description Interval E-value
RfbC COG1898
dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis] ...
1-176 5.43e-120

dTDP-4-dehydrorhamnose 3,5-epimerase or related enzyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441502  Cd Length: 177  Bit Score: 336.27  E-value: 5.43e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   1 MKIIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQT-ENTQGKLVRVVQGAV 79
Cdd:COG1898    1 MKVIETAIPGVLLIEPKVFGDERGFFFETFNAEEFAEAGLDFDFVQDNHSRSRKGVLRGLHFQLpPHAQAKLVRVVRGAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667  80 FDVAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDG 159
Cdd:COG1898   81 FDVAVDLRKGSPTFGQWVGVELSAENGRQLYIPEGFAHGFLTLSDDAEVLYKVTDYYAPEAERGIRWNDPDLGIDWPLPL 160
                        170
                 ....*....|....*..
gi 491797667 160 EPSLSVKDLAGKVLADA 176
Cdd:COG1898  161 EPILSEKDAAAPTLAEA 177
dTDP_sugar_isom pfam00908
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of ...
12-174 3.13e-108

dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.


Pssm-ID: 459991  Cd Length: 164  Bit Score: 305.84  E-value: 3.13e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   12 KLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQT-ENTQGKLVRVVQGAVFDVAVDLRKSS 90
Cdd:pfam00908   1 LLIEPKVFGDERGFFFESFNAEEFAAAGLDVDFVQDNHSRSKKGVLRGLHYQLpPHAQAKLVRVVRGEVFDVAVDLRKGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   91 PTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDGEPSLSVKDLAG 170
Cdd:pfam00908  81 PTFGQWVGVELSAENKRQLYIPEGFAHGFLVLSDDAEVLYKVTEYYAPEHERGIRWNDPDLGIDWPLPDEPILSEKDAAA 160

                  ....
gi 491797667  171 KVLA 174
Cdd:pfam00908 161 PLLA 164
rmlC TIGR01221
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of ...
2-176 3.36e-104

dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of dTDP-L-rhamnose, often as a precursor to LPS O-antigen [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273510  Cd Length: 176  Bit Score: 296.23  E-value: 3.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667    2 KIIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQTENTQGKLVRVVQGAVFD 81
Cdd:TIGR01221   1 NFIRTEIPDVLLIEPRVFGDERGFFMETYNDEAFQEQGIPVRFVQDNHSKSYKGVLRGLHYQRPHPQGKLVRVLRGEVFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   82 VAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDGEP 161
Cdd:TIGR01221  81 VAVDLRRNSPTFGKWVGVLLSAENKRQLWIPEGFAHGFVVLSDEAEFLYKCTDYYAPEYERGIIWNDPDIGIDWPLEDAP 160
                         170
                  ....*....|....*
gi 491797667  162 SLSVKDLAGKVLADA 176
Cdd:TIGR01221 161 ILSEKDRNGPPLAEA 175
cupin_RmlC cd00438
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine ...
3-169 8.48e-104

RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380337  Cd Length: 168  Bit Score: 295.10  E-value: 8.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667   3 IIETKIPDVKLLEPQVFGDERGFFMETFRDEWFRQNVADRTFVQENHSKSIKGVLRGLHYQTE-NTQGKLVRVVQGAVFD 81
Cdd:cd00438    1 FTETAIPGVLLIEPKVFGDERGFFAETFNKEEFAEAGINPDFVQDNHSFSKKGVLRGLHFQLPpHAQAKLVRCLRGAIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491797667  82 VAVDLRKSSPTFGQWVGEVLSAENKRQLWVPEGFAHGFYVLTETAEFTYKCTDYYNPKAEHSLIWNDPTVAIDWNLDgEP 161
Cdd:cd00438   81 VAVDLRKGSPTFGQWVGVELSAENHRQLYIPEGFAHGFQTLSDDAEVLYKCSDYYAPESERGIRWNDPDLGIDWPLP-EP 159

                 ....*...
gi 491797667 162 SLSVKDLA 169
Cdd:cd00438  160 ILSEKDRN 167
 
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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