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Conserved domains on  [gi|2043882021|ref|XP_012430520|]
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ribulose-phosphate 3-epimerase isoform X1 [Taeniopygia guttata]

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 1.24e-78

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: 231.98  E-value: 1.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   1 MHMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429    62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  81 GQKFMEDMMPKVQWLRTQFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 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 1.24e-78

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: 231.98  E-value: 1.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   1 MHMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429    62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  81 GQKFMEDMMPKVQWLRTQFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 146
Cdd:cd00429   142 GQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-148 2.04e-71

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 214.46  E-value: 2.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEA-ADNPGALIKDIRENGMKVGLAIKPGTTVEHLAP--WANQIDMALVMTVEPG 78
Cdd:PTZ00170   71 HLMVSNPEKWVDDFAKAGASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPG 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  79 FGGQKFMEDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNV 148
Cdd:PTZ00170  151 FGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-152 4.23e-66

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: 200.69  E-value: 4.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:COG0036    64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGG 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043882021  82 QKFMEDMMPKVQWLRTQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 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 5.08e-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: 161.73  E-value: 5.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2043882021  82 QKFMEDMMPKVQWLRTQFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 132
Cdd:pfam00834 143 QSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-146 7.45e-47

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: 151.27  E-value: 7.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGG 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043882021  82 QKFMEDMMPKVQWLRT----QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 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 1.24e-78

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: 231.98  E-value: 1.24e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   1 MHMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFG 80
Cdd:cd00429    62 VHLMVENPERYIEAFAKAGADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFG 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  81 GQKFMEDMMPKVQWLRTQFP----SLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 146
Cdd:cd00429   142 GQKFIPEVLEKIRKLRELIPennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 2-148 2.04e-71

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


Pssm-ID: 240303  Cd Length: 228  Bit Score: 214.46  E-value: 2.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEA-ADNPGALIKDIRENGMKVGLAIKPGTTVEHLAP--WANQIDMALVMTVEPG 78
Cdd:PTZ00170   71 HLMVSNPEKWVDDFAKAGASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPliDTDLVDMVLVMTVEPG 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  79 FGGQKFMEDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNV 148
Cdd:PTZ00170  151 FGGQSFMHDMMPKVRELRKRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 2-152 4.23e-66

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: 200.69  E-value: 4.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:COG0036    64 HLMIENPDRYIEAFAEAGADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGG 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043882021  82 QKFMEDMMPKVQWLRTQF----PSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 152
Cdd:COG0036   144 QKFIPSVLEKIRRLRELIdergLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 2-155 4.37e-66

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 201.00  E-value: 4.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAA--DNPGALIKDIRENGMKVGLAIKPGTTVEHLAPW--ANQIDMALVMTVEP 77
Cdd:PLN02334   71 HLMVTNPEDYVPDFAKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVveKGLVDMVLVMSVEP 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043882021  78 GFGGQKFMEDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEAAQK 155
Cdd:PLN02334  151 GFGGQSFIPSMMDKVRALRKKYPELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAAVA 228
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 2-147 5.52e-63

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 192.71  E-value: 5.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:PRK05581   67 HLMVENPDRYVPDFAKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGG 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021  82 QKFMEDMMPKVQWLR----TQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRN 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 5.08e-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: 161.73  E-value: 5.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:pfam00834  63 HLMVEEPDRIIPDFAKAGADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGG 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2043882021  82 QKFMEDMMPKVQWLRTQFPS----LDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 132
Cdd:pfam00834 143 QSFIPSVLEKIRKVRKMIDErgldTLIEVDGGIKLDNIPQIAEAGADVIVAGSAV 197
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 2-146 7.45e-47

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: 151.27  E-value: 7.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:TIGR01163  62 HLMVENPDRYIEDFAEAGADIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGG 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043882021  82 QKFMEDMMPKVQWLRT----QFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 146
Cdd:TIGR01163 142 QKFIPDTLEKIREVRKmideLGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-130 1.15e-28

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 105.46  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPG-ALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFG 80
Cdd:PRK09722   65 HLMVTDPQDYIDQLADAGADFITLHPETINGQAfRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFA 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2043882021  81 GQKFMEDMMPKV----QWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGS 130
Cdd:PRK09722  145 GQPFIPEMLDKIaelkALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGT 198
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
2-142 1.83e-26

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 99.34  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   2 HMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKVGLAIKPGTTVEHLAPWANQIDMALVMTVEPGFGG 81
Cdd:PRK08005   64 HLMVSSPQRWLPWLAAIRPGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRG 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2043882021  82 QKFMEDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 142
Cdd:PRK08005  144 QQFIAAMCEKVSQSREHFPAAECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 1-137 1.45e-09

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 54.50  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   1 MHMMVAAPEQWVKPMAVAGANQYTFHLEAADNPGALIKDIRENGMKV--GLAIKPGTTVEHLAPWANQIDMALVMTVEPG 78
Cdd:PRK08091   73 VHLMVRDQFEVAKACVAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPR 152

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2043882021  79 FGGQKFMEDMMPKVQWLRTQFPSLD----IEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSAD 137
Cdd:PRK08091  153 TGTKAPSDLILDRVIQVENRLGNRRveklISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 108-152 1.63e-05

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: 42.86  E-value: 1.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2043882021 108 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEA 152
Cdd:COG0352   162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 104-142 2.45e-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: 42.57  E-value: 2.45e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2043882021 104 IEVDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 142
Cdd:cd04726   161 VAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 108-146 2.88e-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: 42.12  E-value: 2.88e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2043882021 108 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLR 146
Cdd:cd00564   157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
106-142 3.60e-04

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 39.61  E-value: 3.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2043882021 106 VDGGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVI 142
Cdd:PRK13307  335 VAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAA 371
PRK14057 PRK14057
epimerase; Provisional
 1-143 5.21e-04

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 38.90  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043882021   1 MHMMVAapEQWVKPMAVAGANQYTFHLEAADNP---------GALIKDIRENGMKV--GLAIKPGTTVEHLAPWANQIDM 69
Cdd:PRK14057   80 VHLMVA--DQWTAAQACVKAGAHCITLQAEGDIhlhhtlswlGQQTVPVIGGEMPVirGISLCPATPLDVIIPILSDVEV 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043882021  70 ALVMTVEPGFGGQKFMEDMMPKVQWLRTQFPSLD----IEVDGGVGPDTIHKCAEAGANMIVSGSAIMKsaDPRSVIN 143
Cdd:PRK14057  158 IQLLAVNPGYGSKMRSSDLHERVAQLLCLLGDKRegkiIVIDGSLTQDQLPSLIAQGIDRVVSGSALFR--DDRLVEN 233
thiE PRK00043
thiamine phosphate synthase;
108-153 1.41e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 37.47  E-value: 1.41e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2043882021 108 GGVGPDTIHKCAEAGANMIVSGSAIMKSADPRSVINLLRNVCSEAA 153
Cdd:PRK00043  167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
QRPTase_C pfam01729
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ...
 86-132 2.27e-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: 36.52  E-value: 2.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2043882021  86 EDMMPKVQWLRTQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGSAI 132
Cdd:pfam01729 112 EEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALT 158
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 86-130 2.54e-03

Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It 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. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.


Pssm-ID: 238802 [Multi-domain]  Cd Length: 269  Bit Score: 37.07  E-value: 2.54e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2043882021  86 EDMMPKVQWLRtQFPSLDIEVDGGVGPDTIHKCAEAGANMIVSGS 130
Cdd:cd01568   213 EELKEAVKLLK-GLPRVLLEASGGITLENIRAYAETGVDVISTGA 256
 
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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