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Conserved domains on  [gi|1021858607|ref|WP_063392004|]
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ribulose-phosphate 3-epimerase [Ralstonia mannitolilytica]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10784968)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
10-240 2.11e-134

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


:

Pssm-ID: 439806  Cd Length: 218  Bit Score: 377.11  E-value: 2.11e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  10 FRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvPIDVHLMVRPVDRIIP 89
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDL-----PLDVHLMIENPDRYIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  90 DFAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:COG0036    76 AFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021858607 170 AVRQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAGV 240
Cdd:COG0036   156 RLRELID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAAAAA 218
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
10-240 2.11e-134

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 377.11  E-value: 2.11e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  10 FRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvPIDVHLMVRPVDRIIP 89
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDL-----PLDVHLMIENPDRYIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  90 DFAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:COG0036    76 AFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021858607 170 AVRQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAGV 240
Cdd:COG0036   156 RLRELID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
10-239 1.50e-128

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 362.19  E-value: 1.50e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  10 FRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvPIDVHLMVRPVDRIIP 89
Cdd:PRK05581    4 VLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKL-----PLDVHLMVENPDRYVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  90 DFAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:PRK05581   79 DFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607 170 AVRQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAG 239
Cdd:PRK05581  159 ELRKLID----ERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAELAA 220
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
12-221 2.75e-121

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 343.49  E-value: 2.75e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQkdgkpVPIDVHLMVRPVDRIIPDF 91
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTD-----LPIDVHLMVENPDRYIEDF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAV 171
Cdd:TIGR01163  76 AEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021858607 172 RQKLDAYqeksGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPD 221
Cdd:TIGR01163 156 RKMIDEL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
12-234 1.05e-118

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 337.14  E-value: 1.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQkdgkpVPIDVHLMVRPVDRIIPDF 91
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTD-----LPLDVHLMVENPERYIEAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAV 171
Cdd:cd00429    77 AKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021858607 172 RQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALR 234
Cdd:cd00429   157 RELIP----ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
11-217 4.79e-113

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 322.36  E-value: 4.79e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  11 RIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAqkdgkPVPIDVHLMVRPVDRIIPD 90
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLT-----DLPLDVHLMVEEPDRIIPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  91 FAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRA 170
Cdd:pfam00834  76 FAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1021858607 171 VRQKLDAYqeksGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVF 217
Cdd:pfam00834 156 VRKMIDER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
10-240 2.11e-134

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 377.11  E-value: 2.11e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  10 FRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvPIDVHLMVRPVDRIIP 89
Cdd:COG0036     1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDL-----PLDVHLMIENPDRYIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  90 DFAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:COG0036    76 AFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIR 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021858607 170 AVRQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAGV 240
Cdd:COG0036   156 RLRELID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAAAAA 218
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
10-239 1.50e-128

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 362.19  E-value: 1.50e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  10 FRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvPIDVHLMVRPVDRIIP 89
Cdd:PRK05581    4 VLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKL-----PLDVHLMVENPDRYVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  90 DFAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:PRK05581   79 DFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607 170 AVRQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAG 239
Cdd:PRK05581  159 ELRKLID----ERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAELAA 220
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
12-221 2.75e-121

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 343.49  E-value: 2.75e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQkdgkpVPIDVHLMVRPVDRIIPDF 91
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTD-----LPIDVHLMVENPDRYIEDF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAV 171
Cdd:TIGR01163  76 AEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREV 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021858607 172 RQKLDAYqeksGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPD 221
Cdd:TIGR01163 156 RKMIDEL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
12-234 1.05e-118

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 337.14  E-value: 1.05e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQkdgkpVPIDVHLMVRPVDRIIPDF 91
Cdd:cd00429     2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTD-----LPLDVHLMVENPERYIEAF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAV 171
Cdd:cd00429    77 AKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021858607 172 RQKLDayqeKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALR 234
Cdd:cd00429   157 RELIP----ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
11-217 4.79e-113

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 322.36  E-value: 4.79e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  11 RIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAqkdgkPVPIDVHLMVRPVDRIIPD 90
Cdd:pfam00834   1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLT-----DLPLDVHLMVEEPDRIIPD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  91 FAKAGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRA 170
Cdd:pfam00834  76 FAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1021858607 171 VRQKLDAYqeksGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVF 217
Cdd:pfam00834 156 VRKMIDER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
11-242 1.61e-108

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 311.94  E-value: 1.61e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  11 RIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQkdgkpVPIDVHLMVRPVDRIIPD 90
Cdd:PLN02334    9 IIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTD-----APLDCHLMVTNPEDYVPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  91 FAKAGADLITFHPEAS--EHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMD--RLDMVLIMSVNPGFGGQSFIPEALN 166
Cdd:PLN02334   84 FAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMD 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021858607 167 KLRAVRQKLDAyqeksgrkILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDadggYRGTVGALRQALAGVGA 242
Cdd:PLN02334  164 KVRALRKKYPE--------LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPD----YAEVISGLRASVEKAAV 227
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
12-221 2.62e-72

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 220.24  E-value: 2.62e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpVPIDVHLMVRPVDRIIPDF 91
Cdd:PTZ00170    9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPN----TFLDCHLMVSNPEKWVDDF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLA-LIRDNGCKAGLVFNPATPLHYLDHVMDR--LDMVLIMSVNPGFGGQSFIPEALNKL 168
Cdd:PTZ00170   85 AKAGASQFTFHIEATEDDPKAVArKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKV 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1021858607 169 RAVRQKLdayqeksgRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPD 221
Cdd:PTZ00170  165 RELRKRY--------PHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKD 209
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
12-218 3.40e-66

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 204.46  E-value: 3.40e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRrVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAqkdgkPVPIDVHLMVRPVDRIIPDF 91
Cdd:PRK09722    5 ISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLA-----SKPLDVHLMVTDPQDYIDQL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPE-ASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRA 170
Cdd:PRK09722   79 ADAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1021858607 171 VRQkldaYQEKSGRKILLEIDGGVKADNIAEIARAGADTFVAG-SAVFG 218
Cdd:PRK09722  159 LKA----LRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFN 203
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
14-223 1.75e-28

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 107.05  E-value: 1.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  14 PSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAqkdgkPVPIDVHLMVRPVDRIIPDFAK 93
Cdd:PRK08005    5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQT-----RHPLSFHLMVSSPQRWLPWLAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  94 AGADLITFHPEASEHIDRSLALIRDNGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAVRQ 173
Cdd:PRK08005   80 IRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSRE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021858607 174 KLDAYQEKSgrkilleiDGGVKADNIAEIARAGADTFVAGSAVFGKPDAD 223
Cdd:PRK08005  160 HFPAAECWA--------DGGITLRAARLLAAAGAQHLVIGRALFTTANYD 201
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
12-223 7.81e-20

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 84.54  E-value: 7.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  12 IAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKdgkpvpiDVHLMVRPVDRIIPDF 91
Cdd:PRK08091   15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK-------DVHLMVRDQFEVAKAC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  92 AKAGADLITFHPEASEHIDRSLALIRDNGCKA--GLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLR 169
Cdd:PRK08091   88 VAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVI 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1021858607 170 AVRQKL-DAYQEKsgrkiLLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDAD 223
Cdd:PRK08091  168 QVENRLgNRRVEK-----LISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELK 217
PRK14057 PRK14057
epimerase; Provisional
8-217 3.48e-13

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 67.02  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607   8 SGFRIAPSILSADFARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEAIRPHAQKDgkpvpidVHLMVRPVDRI 87
Cdd:PRK14057   18 ASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIKD-------VHLMVADQWTA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  88 IPDFAKAGADLITFHPEASEHIDRSLALIRDNGCKA---------GLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQ 158
Cdd:PRK14057   91 AQACVKAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSK 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858607 159 SFIPEALNKlraVRQKLDAYQEKSGRKILLeIDGGVKADNIAEIARAGADTFVAGSAVF 217
Cdd:PRK14057  171 MRSSDLHER---VAQLLCLLGDKREGKIIV-IDGSLTQDQLPSLIAQGIDRVVSGSALF 225
PRTase_typeII cd00516
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ...
159-227 1.55e-05

Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an important role in NAD production by either allowing quinolinic acid (QA) , quinolinate phosphoribosyl transferase (QAPRTase), or nicotinic acid (NA), nicotinate phosphoribosyltransferase (NAPRTase), to be used in the synthesis of NAD. QAPRTase catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide, an important step in the de novo synthesis of NAD. NAPRTase catalyses a similar reaction leading to NAMN and pyrophosphate, using nicotinic acid an PPRP as substrates, used in the NAD salvage pathway.


Pssm-ID: 238286 [Multi-domain]  Cd Length: 281  Bit Score: 44.92  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021858607 159 SFIPEALNKLRAVRQKLDAYQEKSGRKILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKPDADGGYR 227
Cdd:cd00516   213 SGSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
192-240 9.26e-04

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 39.01  E-value: 9.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1021858607 192 GGVKADNIAEIARAGADTFVAGSAVFGKPDAdggyRGTVGALRQALAGV 240
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDP----AAAARELRAALEAA 206
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
22-214 2.31e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 37.95  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  22 ARLGEEVRRVLESGADWIHFDVMDNHYVPNLTVGPLVCEairphAQKDGKPVPIDVHLMVRPVDRIIPDFAK----AGAD 97
Cdd:cd04722    12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLK-----EVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGAD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021858607  98 LITFHPEASEHIDRSLALIRD-----NGCKAGLVFNPATPLHYLDHVMDRLDMVLIMSVNPGFGGQSFIPEALNKLRAVR 172
Cdd:cd04722    87 GVEIHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAK 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1021858607 173 QKLdayqeksgrKILLEIDGGVK-ADNIAEIARAGADTFVAGS 214
Cdd:cd04722   167 RGS---------KVPVIAGGGINdPEDAAEALALGADGVIVGS 200
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
192-221 3.11e-03

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 37.50  E-value: 3.11e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1021858607 192 GGVKADNIAEIARAGADTFVAGSAVFGKPD 221
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADD 186
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
160-220 3.13e-03

ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide.


Pssm-ID: 238807 [Multi-domain]  Cd Length: 272  Bit Score: 38.05  E-value: 3.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021858607 160 FIPEALNKLRavrQKLDAYQEKsgrkILLEIDGGVKADNIAEIARAGADTFVAGSAVFGKP 220
Cdd:cd01573   212 FSPEELAELV---PKLRSLAPP----VLLAAAGGINIENAAAYAAAGADILVTSAPYYAKP 265
 
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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