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Conserved domains on  [gi|514062315|ref|WP_016528626|]
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L-fucose mutarotase [Glaesserella parasuis]

Protein Classification

RbsD/FucU family protein( domain architecture ID 10008334)

RbsD/FucU family protein similar to Streptococcus pneumoniae fucose mutarotase, a component of the fucose-utilization pathway, which catalyzes the interconversion between alpha-L-fucose and beta-L-fucose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
1-142 5.00e-81

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


:

Pssm-ID: 443323  Cd Length: 143  Bit Score: 235.06  E-value: 5.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVERPLAMMQAVPGD 80
Cdd:COG4154    1 MLKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAESLARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVGGP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062315  81 SLDPAVEERYLAAIAKINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVTP 142
Cdd:COG4154   81 DEVPPVWAEYQAIIAKAEGRPVPIERLERFAFYERAKKAYAVVATGETRLYGNIILKKGVIP 142
 
Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
1-142 5.00e-81

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


Pssm-ID: 443323  Cd Length: 143  Bit Score: 235.06  E-value: 5.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVERPLAMMQAVPGD 80
Cdd:COG4154    1 MLKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAESLARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVGGP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062315  81 SLDPAVEERYLAAIAKINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVTP 142
Cdd:COG4154   81 DEVPPVWAEYQAIIAKAEGRPVPIERLERFAFYERAKKAYAVVATGETRLYGNIILKKGVIP 142
fucU PRK15420
L-fucose mutarotase; Provisional
1-142 5.61e-67

L-fucose mutarotase; Provisional


Pssm-ID: 185318  Cd Length: 140  Bit Score: 199.33  E-value: 5.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVErPLAMMQAVPGD 80
Cdd:PRK15420   1 MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAP-PLVMMAAVEGD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062315  81 SLDPAVEERYLAAIAkINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVTP 142
Cdd:PRK15420  80 TLDPEVERRYRNALS-LQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP 140
RbsD_FucU pfam05025
RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport ...
3-141 1.06e-51

RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport system consists of six proteins encoded by the rbs operon (rbsD, rbsA, rbsC, rbsB, rbsK and rbsR). RbsD was originally thought to be a high affinity ribose transport protein, but further analysis shows that it is a D-ribose pyranase. It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. This family also includes FucU a component of the fucose operon and is a L-fucose mutarotase, involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose. Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organizms from eubacteria to mammals.


Pssm-ID: 428264  Cd Length: 132  Bit Score: 160.27  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315    3 KGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKV---IRADGIQIATLLEAITPLFEYD-QYVERPlammqAVP 78
Cdd:pfam05025   1 MKKSGILNPELLKVLAEMGHGDEIVIADAGFPIPSGVERIdlaLRAGGPSFLDVLDAVLSELPVEkVYVAEE-----IVE 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514062315   79 GDsldPAVEERYLAAIAKINGKaplVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVT 141
Cdd:pfam05025  76 GN---PEVWAEYLALLPKAEGE---IEYVEHEAFKERAKKAKAVVRTGETTPYANIILKKGVV 132
 
Name Accession Description Interval E-value
FucU COG4154
L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];
1-142 5.00e-81

L-fucose mutarotase/ribose pyranase, RbsD/FucU family [Carbohydrate transport and metabolism];


Pssm-ID: 443323  Cd Length: 143  Bit Score: 235.06  E-value: 5.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVERPLAMMQAVPGD 80
Cdd:COG4154    1 MLKGIDPLLSPELLKVLAEMGHGDEIVLADANFPAESLARRVVRLDGHSAPELLEAILSLFPLDTFVDDPVVRMEVVGGP 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062315  81 SLDPAVEERYLAAIAKINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVTP 142
Cdd:COG4154   81 DEVPPVWAEYQAIIAKAEGRPVPIERLERFAFYERAKKAYAVVATGETRLYGNIILKKGVIP 142
fucU PRK15420
L-fucose mutarotase; Provisional
1-142 5.61e-67

L-fucose mutarotase; Provisional


Pssm-ID: 185318  Cd Length: 140  Bit Score: 199.33  E-value: 5.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKVIRADGIQIATLLEAITPLFEYDQYVErPLAMMQAVPGD 80
Cdd:PRK15420   1 MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAP-PLVMMAAVEGD 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514062315  81 SLDPAVEERYLAAIAkINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVTP 142
Cdd:PRK15420  80 TLDPEVERRYRNALS-LQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP 140
RbsD_FucU pfam05025
RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport ...
3-141 1.06e-51

RbsD / FucU transport protein family; The Escherichia coli high-affinity ribose-transport system consists of six proteins encoded by the rbs operon (rbsD, rbsA, rbsC, rbsB, rbsK and rbsR). RbsD was originally thought to be a high affinity ribose transport protein, but further analysis shows that it is a D-ribose pyranase. It catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. This family also includes FucU a component of the fucose operon and is a L-fucose mutarotase, involved in the anomeric conversion of L-fucose. It also exhibits a pyranase activity for D-ribose. Both have been classified in the RbsD/FucU family of proteins. Members of this family are ubiquitous having been found in organizms from eubacteria to mammals.


Pssm-ID: 428264  Cd Length: 132  Bit Score: 160.27  E-value: 1.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315    3 KGIHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKV---IRADGIQIATLLEAITPLFEYD-QYVERPlammqAVP 78
Cdd:pfam05025   1 MKKSGILNPELLKVLAEMGHGDEIVIADAGFPIPSGVERIdlaLRAGGPSFLDVLDAVLSELPVEkVYVAEE-----IVE 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514062315   79 GDsldPAVEERYLAAIAKINGKaplVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGVT 141
Cdd:pfam05025  76 GN---PEVWAEYLALLPKAEGE---IEYVEHEAFKERAKKAKAVVRTGETTPYANIILKKGVV 132
RbsD COG1869
D-ribose pyranose/furanose isomerase RbsD [Carbohydrate transport and metabolism];
1-140 1.38e-13

D-ribose pyranose/furanose isomerase RbsD [Carbohydrate transport and metabolism];


Pssm-ID: 441474  Cd Length: 129  Bit Score: 63.18  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   1 MLKgiHPALSPELLKVLAEMGHGDEIVLSDAHFPAHQLHHKV---IRADGIQIATLLEAITPLFEydqyVERPLaMMQAV 77
Cdd:COG1869    1 MKK--TGILNSELSRVLARLGHTDTIVIADAGLPIPPGVERIdlaLTPGVPSFLDVLDAVLSELQ----VEKAI-LAEEI 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514062315  78 PGDSldPAVEERYLAAIAKINgkaplVERVERFAFYDRAKTAYAVVITGELAKYGNIILKKGV 140
Cdd:COG1869   74 KEKN--PELHEALLELLPGIE-----IEYVSHEEFKELTKQAKAVIRTGECTPYANIILVSGV 129
PRK11797 PRK11797
D-ribose pyranase; Provisional
6-141 7.39e-07

D-ribose pyranase; Provisional


Pssm-ID: 183318  Cd Length: 139  Bit Score: 45.60  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315   6 HPALSPELLKVLAEMGHGDEIVLSDAHFPahqlhhkvIRADgiqiatlleaitplfeydqyVER-PLAMMQAVPG--DSL 82
Cdd:PRK11797   4 TGLLNSEISSVIARLGHTDTLVICDAGLP--------IPNG--------------------VERiDLALTKGVPSflDVL 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514062315  83 DP-----AVEERYLA-------------------AIAKINGKAPLVERVERFAFYDRAKTAYAVVITGELAKYGNIILKK 138
Cdd:PRK11797  56 DVvlsemQVEKAILAeeikehnpelhealltqleQLEQHQGNTIEIEYVSHEEFKQLTAESKAVIRTGECTPYANIILES 135

                 ...
gi 514062315 139 GVT 141
Cdd:PRK11797 136 GVT 138
 
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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