|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-211 |
2.16e-118 |
|
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: 335.51 E-value: 2.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 4 PIIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKA 81
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVeaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 82 GASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRER 161
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843685 162 IDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAA 210
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-211 |
8.65e-118 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 334.07 E-value: 8.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 1 MSAPIIAPSILAADFARLDREVEAVAN--ADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTY 78
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAagADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 79 IKAGASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKL 158
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740843685 159 RERIDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDS 213
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-211 |
3.24e-113 |
|
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: 322.12 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 5 IIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLeeAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERI 162
Cdd:cd00429 81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740843685 163 DAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKE 209
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-210 |
5.29e-94 |
|
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: 273.77 E-value: 5.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 6 IAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAGA 83
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVeeAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 84 SSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERID 163
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740843685 164 AEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVD 210
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIR 207
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
5-200 |
7.90e-90 |
|
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: 262.65 E-value: 7.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 5 IIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVenAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERI 162
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 740843685 163 DAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-211 |
2.16e-118 |
|
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: 335.51 E-value: 2.16e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 4 PIIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKA 81
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVeaAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 82 GASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRER 161
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843685 162 IDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAA 210
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-211 |
8.65e-118 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 334.07 E-value: 8.65e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 1 MSAPIIAPSILAADFARLDREVEAVAN--ADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTY 78
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAagADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 79 IKAGASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKL 158
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740843685 159 RERIDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDS 213
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
5-211 |
3.24e-113 |
|
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: 322.12 E-value: 3.24e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 5 IIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLeeAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERI 162
Cdd:cd00429 81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740843685 163 DAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKE 209
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-210 |
5.29e-94 |
|
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: 273.77 E-value: 5.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 6 IAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAGA 83
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVeeAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 84 SSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERID 163
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740843685 164 AEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVD 210
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIR 207
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
4-211 |
9.25e-93 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 271.09 E-value: 9.25e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 4 PIIAPSILAADFARLDREVEAVAN--ADWLHIDVMDGHFVPNLSFGAPVLEAV-AAVTDKYLDVHLMIENPEKWVDTYIK 80
Cdd:PTZ00170 7 AIIAPSILAADFSKLADEAQDVLSggADWLHVDVMDGHFVPNLSFGPPVVKSLrKHLPNTFLDCHLMVSNPEKWVDDFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 81 AGASSVIFHVEA-ADDAIALARHIRSQGVKAGFSLRPGTPIE---PWLDhLAEFDEVLVMSVEPGFGGQSFMPDQLAKVE 156
Cdd:PTZ00170 87 AGASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEvlfPLID-TDLVDMVLVMTVEPGFGGQSFMHDMMPKVR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740843685 157 KLRERIDaeglDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:PTZ00170 166 ELRKRYP----HLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIEL 216
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-210 |
1.18e-92 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 271.10 E-value: 1.18e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 1 MSAPIIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTY 78
Cdd:PLN02334 5 KNDAIIAPSILSADFANLAEEAKRVldAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 79 IKAGASSVIFHVEAA--DDAIALARHIRSQGVKAGFSLRPGTPIE---PWLDhLAEFDEVLVMSVEPGFGGQSFMPDQLA 153
Cdd:PLN02334 85 AKAGASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEavePVVE-KGLVDMVLVMSVEPGFGGQSFIPSMMD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740843685 154 KVEKLRERIDaeglDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVD 210
Cdd:PLN02334 164 KVRALRKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVIS 216
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
5-200 |
7.90e-90 |
|
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: 262.65 E-value: 7.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 5 IIAPSILAADFARLDREVEAV--ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVenAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERI 162
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 740843685 163 DAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVF 200
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
4-204 |
1.13e-60 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 189.82 E-value: 1.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 4 PIIAPSILAADFARLDREVEAV-ANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:PRK09722 3 MKISPSLMCMDLLKFKEQIEFLnSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAAD-DAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRER 161
Cdd:PRK09722 83 ADFITLHPETINgQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 740843685 162 IDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAG-SAVFGADD 204
Cdd:PRK09722 163 RERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDE 206
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
5-211 |
4.17e-36 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 126.31 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 5 IIAPSILAADFARLDREVEAVANADW--LHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDTYIKAG 82
Cdd:PRK08005 2 ILHPSLASADPLRYAEALTALHDAPLgsLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 83 ASSVIFHVEAADDAIALARHIRSQGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRERI 162
Cdd:PRK08005 82 PGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740843685 163 DAegldTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:PRK08005 162 PA----AECWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQ 206
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
6-211 |
8.16e-18 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 78.76 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 6 IAPSILAADFARLDREVEAVA--NADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKylDVHLMIENPEKWVDTYIKAGA 83
Cdd:PRK08091 15 ISVGILASNWLKFNETLTTLSenQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK--DVHLMVRDQFEVAKACVAAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 84 SSVIFHVEAADDAIALARHIRSQ--GVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVEKLRER 161
Cdd:PRK08091 93 DIVTLQVEQTHDLALTIEWLAKQktTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVENR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740843685 162 IDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:PRK08091 173 LGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKE 222
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
10-205 |
2.24e-14 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 69.71 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 10 ILAADFARLDR---EVEAVaNADWLHIDVMDGHFVPNLSFGApvlEAVAAVTDKYL-DVHLMIENPEKWVDTYIKAGASS 85
Cdd:PRK14057 26 ILAGQWIALHRylqQLEAL-NQPLLHLDLMDGQFCPQFTVGP---WAVGQLPQTFIkDVHLMVADQWTAAQACVKAGAHC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 86 VIFHVEAADDAIALARHIRSQGVKA---------GFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPDQLAKVE 156
Cdd:PRK14057 102 ITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740843685 157 KLRERIDAEGLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFgADDR 205
Cdd:PRK14057 182 QLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF-RDDR 229
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
12-197 |
1.41e-04 |
|
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: 41.42 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 12 AADFARLDREVEAVANADWLHIDVMDGHFVPNLSFGAPVLEAVAAVTDKYLDVHLMIENPEKWVDT----YIKAGASSVI 87
Cdd:cd04722 10 PSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIaaaaARAAGADGVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 88 FHVEAADDAIALARHIRS-----QGVKAGFSLRPGTPIEPWLDHLAEFDEVLVMSVEPGFGGQSFMPdqlakVEKLRERI 162
Cdd:cd04722 90 IHGAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVP-----IADLLLIL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 740843685 163 DAEGLDTLIEIDGGI-SAKTIESAAAAGCDAFVAGS 197
Cdd:cd04722 165 AKRGSKVPVIAGGGInDPEDAAEALALGADGVIVGS 200
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
175-209 |
1.10e-03 |
|
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: 38.63 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*
gi 740843685 175 GGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAV 209
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAA 196
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
175-211 |
2.79e-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: 2.79e-03
10 20 30
....*....|....*....|....*....|....*..
gi 740843685 175 GGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARE 193
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
143-211 |
3.50e-03 |
|
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: 37.17 E-value: 3.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843685 143 GGQSFMPDQLAKVEKLreridaegLDTLIEIDGGISAKTIESAAAAGCDAFVAGSAVFGADDRAAAVDE 211
Cdd:cd04726 141 AGGWWPEDDLKKVKKL--------LGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAARE 201
|
|
| HisA_HisF |
cd04723 |
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
68-199 |
5.55e-03 |
|
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.
Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 36.86 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843685 68 IENPEKWVdtyiKAGASSVIFHVEAADDAI---ALARHIRSQGV-----KAGFSLRPGTPIEP--WLDHLAEF-DEVLVM 136
Cdd:cd04723 90 LENAQEWL----KRGASRVIVGTETLPSDDdedRLAALGEQRLVlsldfRGGQLLKPTDFIGPeeLLRRLAKWpEELIVL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740843685 137 --SVEPGFGGqsfmPDqLAKVEKLRERIDAegldTLIEIDGGISAKTIESAAAAGCDAFVAGSAV 199
Cdd:cd04723 166 diDRVGSGQG----PD-LELLERLAARADI----PVIAAGGVRSVEDLELLKKLGASGALVASAL 221
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
144-203 |
9.26e-03 |
|
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: 36.45 E-value: 9.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740843685 144 GQSFMPDQLAKVEKLRERIDAEGLDT-LIEIDGGISAKTIESAAAAGCDAFVAGSAVFGAD 203
Cdd:cd00516 214 GSPEELDPAVLILKARAHLDGKGLPRvKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAP 274
|
|
| |
