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Conserved domains on  [gi|974576746|ref|NP_001305860|]
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ribulose-phosphate 3-epimerase isoform 4 [Homo sapiens]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10087218)

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

EC:  5.1.3.1
Gene Ontology:  GO:0046872|GO:0004750

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 1-146 3.29e-81

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: 238.53  E-value: 3.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  81 GQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:cd00429  142 GQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 1-146 3.29e-81

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: 238.53  E-value: 3.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  81 GQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:cd00429  142 GQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-148 2.42e-73

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 219.47  E-value: 2.42e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTSVEYLAP--WANQIDMALVMTVEPG 78
Cdd:PTZ00170  71 HLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPG 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  79 FGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 148
Cdd:PTZ00170 151 FGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-152 2.36e-68

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: 206.08  E-value: 2.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:COG0036   64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGG 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974576746  82 QKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 152
Cdd:COG0036  144 QKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-132 2.20e-51

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: 162.50  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 974576746   82 QKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 132
Cdd:pfam00834 143 QSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-146 8.95e-50

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: 158.98  E-value: 8.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGG 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974576746   82 QKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:TIGR01163 142 QKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
 
Name Accession Description Interval E-value
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 1-146 3.29e-81

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: 238.53  E-value: 3.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429   62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  81 GQKFMEDMMPKVHWLRTQFP----SLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:cd00429  142 GQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-148 2.42e-73

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 219.47  E-value: 2.42e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATEN-PGALIKDIRENGMKVGLAIKPGTSVEYLAP--WANQIDMALVMTVEPG 78
Cdd:PTZ00170  71 HLMVSNPEKWVDDFAKAGASQFTFHIEATEDdPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPG 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  79 FGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNV 148
Cdd:PTZ00170 151 FGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-152 2.36e-68

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: 206.08  E-value: 2.36e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:COG0036   64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGG 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 974576746  82 QKFMEDMMPKVHWLRTQF----PSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 152
Cdd:COG0036  144 QKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-155 1.03e-67

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 205.24  E-value: 1.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLE--ATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPW--ANQIDMALVMTVEP 77
Cdd:PLN02334  71 HLMVTNPEDYVPDFAKAGASIFTFHIEqaSTIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEP 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 974576746  78 GFGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQK 155
Cdd:PLN02334 151 GFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 2-147 1.20e-63

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 194.25  E-value: 1.20e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:PRK05581  67 HLMVENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGG 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746  82 QKFMEDMMPKVHWLR----TQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRN 147
Cdd:PRK05581 147 QKFIPEVLEKIRELRklidERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 2-132 2.20e-51

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: 162.50  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 974576746   82 QKFMEDMMPKVHWLRTQFPS----LDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 132
Cdd:pfam00834 143 QSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-146 8.95e-50

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: 158.98  E-value: 8.95e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746    2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGG 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGG 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 974576746   82 QKFMEDMMPKVHWLRT----QFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:TIGR01163 142 QKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-130 4.28e-28

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 103.92  E-value: 4.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEaTENPGA--LIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGF 79
Cdd:PRK09722  65 HLMVTDPQDYIDQLADAGADFITLHPE-TINGQAfrLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGF 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 974576746  80 GGQKFMEDMMPKV----HWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGS 130
Cdd:PRK09722 144 AGQPFIPEMLDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
2-142 1.73e-25

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 96.64  E-value: 1.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   2 HMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEylaPW---ANQIDMALVMTVEPG 78
Cdd:PRK08005  64 HLMVSSPQRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLL---PYrylALQLDALMIMTSEPD 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 974576746  79 FGGQKFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 142
Cdd:PRK08005 141 GRGQQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 1-137 8.54e-10

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 55.27  E-value: 8.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   1 MHMMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKV--GLAIKPGTSVEYLAPWANQIDMALVMTVEPG 78
Cdd:PRK08091  73 VHLMVRDQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPR 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 974576746  79 FGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSED 137
Cdd:PRK08091 153 TGTKAPSDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 108-152 2.73e-06

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: 45.18  E-value: 2.73e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 974576746 108 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEA 152
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 108-146 1.84e-05

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: 42.89  E-value: 1.84e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 974576746 108 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLR 146
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 104-142 4.24e-05

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 41.80  E-value: 4.24e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 974576746 104 IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 142
Cdd:cd04726  161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
106-142 1.82e-04

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 40.38  E-value: 1.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 974576746 106 VDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 142
Cdd:PRK13307 335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
thiE PRK00043
thiamine phosphate synthase;
108-153 2.13e-04

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 39.78  E-value: 2.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 974576746 108 GGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAA 153
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
PRK14057 PRK14057
epimerase; Provisional
 1-136 2.15e-04

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 40.05  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 974576746   1 MHMMVSkpEQWVKPMAV--AGANQYTFHLEATENPGALIKDIRENGMKV---------GLAIKPGTSVEYLAPWANQIDM 69
Cdd:PRK14057  80 VHLMVA--DQWTAAQACvkAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEV 157

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 974576746  70 ALVMTVEPGFGGQKFMEDMMPKVHWLRTQFPSLD----IEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSE 136
Cdd:PRK14057 158 IQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDD 228
IGPS pfam00218
Indole-3-glycerol phosphate synthase;
112-142 3.26e-03

Indole-3-glycerol phosphate synthase;


Pssm-ID: 395163  Cd Length: 252  Bit Score: 36.51  E-value: 3.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 974576746  112 PDTVHKCAEAGANMIVSGSAIMRSEDPRSVI 142
Cdd:pfam00218 220 PADVRELKEHGANAFLVGESLMRQEDVRAAI 250
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 86-132 6.90e-03

Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold.


Pssm-ID: 396337  Cd Length: 169  Bit Score: 35.36  E-value: 6.90e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 974576746   86 EDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAI 132
Cdd:pfam01729 112 EEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
 
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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