|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
16-238 |
3.30e-130 |
|
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: 366.32 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 16 IRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 96 GANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARAR 175
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1618902835 176 IDrqvaAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAA 215
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
13-238 |
2.56e-122 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 346.40 E-value: 2.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 13 QRAIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMF 92
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 93 AKAGANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQA 172
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1618902835 173 RARIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PRK05581 161 RKLIDE----RGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAEL 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
18-222 |
4.54e-117 |
|
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: 332.70 E-value: 4.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1618902835 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
17-218 |
3.60e-116 |
|
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: 330.06 E-value: 3.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 17 RLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAG 96
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 97 ANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARI 176
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1618902835 177 DRQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
18-235 |
4.36e-115 |
|
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: 327.90 E-value: 4.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1618902835 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLR 235
Cdd:cd00429 162 EN----NLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
16-238 |
3.30e-130 |
|
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: 366.32 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 16 IRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 96 GANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARAR 175
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1618902835 176 IDrqvaAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAED----YAAAIAALREAA 215
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
13-238 |
2.56e-122 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 346.40 E-value: 2.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 13 QRAIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMF 92
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 93 AKAGANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQA 172
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1618902835 173 RARIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PRK05581 161 RKLIDE----RGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPD----YKEAIDSLRAEL 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
18-222 |
4.54e-117 |
|
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: 332.70 E-value: 4.54e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1618902835 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADD 201
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
17-218 |
3.60e-116 |
|
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: 330.06 E-value: 3.60e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 17 RLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAG 96
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 97 ANLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARI 176
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1618902835 177 DRQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
18-235 |
4.36e-115 |
|
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: 327.90 E-value: 4.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1618902835 178 RQvaagGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLR 235
Cdd:cd00429 162 EN----NLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDD----YAEAIKELR 211
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
15-237 |
2.10e-99 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 288.82 E-value: 2.10e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 15 AIRLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAK 94
Cdd:PLN02334 7 DAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 95 AGANLISFHPEASR--HVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDK--LDLVLLMSVNPGFGGQAFIPGVLDKVR 170
Cdd:PLN02334 87 AGASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMDKVR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1618902835 171 QARARIDRqvaaggrpVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREA 237
Cdd:PLN02334 167 ALRKKYPE--------LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPD----YAEVISGLRAS 221
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
16-222 |
1.08e-66 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 205.61 E-value: 1.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 16 IRLAPSILSADFARLGEEVCAIEAGgADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKA 95
Cdd:PRK09722 3 MKISPSLMCMDLLKFKEQIEFLNSK-ADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 96 GANLISFHPE-ASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARA 174
Cdd:PRK09722 82 GADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELKA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1618902835 175 RIDRqvaaGGRPVWLEIDGGVKADNITEIARAGADTFVAG-SAVFGAPD 222
Cdd:PRK09722 162 LRER----NGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDE 206
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
11-238 |
8.48e-64 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 198.29 E-value: 8.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 11 GSQRAIrLAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRP-LVSIPIDVHLMVEPVDALI 89
Cdd:PTZ00170 3 QPLKAI-IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKhLPNTFLDCHLMVSNPEKWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 90 PMFAKAGANLISFHPEA-SRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDK--LDLVLLMSVNPGFGGQAFIPGVL 166
Cdd:PTZ00170 82 DDFAKAGASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1618902835 167 DKVRQARAR---IDRQVaaggrpvwleiDGGVKADNITEIARAGADTFVAGSAVFGAPDadggYRGILHRLREAA 238
Cdd:PTZ00170 162 PKVRELRKRyphLNIQV-----------DGGINLETIDIAADAGANVIVAGSSIFKAKD----RKQAIELLRESV 221
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
18-224 |
5.30e-28 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 105.89 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAKAGA 97
Cdd:PRK08005 3 LHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARID 177
Cdd:PRK08005 83 GWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1618902835 178 RQvaaggrPVWleIDGGVKADNITEIARAGADTFVAGSAVFGAPDAD 224
Cdd:PRK08005 163 AA------ECW--ADGGITLRAARLLAAAGAQHLVIGRALFTTANYD 201
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
22-224 |
1.26e-19 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 84.16 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 22 ILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLvceAIRPLVSIPI-DVHLMVEPVDALIPMFAKAGANLI 100
Cdd:PRK08091 19 ILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAI---AIKQFPTHCFkDVHLMVRDQFEVAKACVAAGADIV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 101 SFHPEASRHVDRTIGLIRDHGCKA--GLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQararIDR 178
Cdd:PRK08091 96 TLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQ----VEN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1618902835 179 QVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDAD 224
Cdd:PRK08091 172 RLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELK 217
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
18-218 |
2.24e-13 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 67.40 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 18 LAPSILSADFARLGEEVCAIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIrPLVSIPiDVHLMVEPVDALIPMFAKAGA 97
Cdd:PRK14057 22 LSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQACVKAGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 98 NLISFHPEASRHVDRTIGLIRDHGCKA---------GLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDK 168
Cdd:PRK14057 100 HCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHER 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1618902835 169 VRQARARIDRQVAAGgrpvWLEIDGGVKADNITEIARAGADTFVAGSAVF 218
Cdd:PRK14057 180 VAQLLCLLGDKREGK----IIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
36-215 |
3.59e-05 |
|
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: 43.34 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 36 AIEAGGADLVHFDVMDNHYVSNLTIGPLVCEAIRPLVSIPIDVHLMVEPVDALIPMFAK----AGANLISFHPEASRHVD 111
Cdd:cd04722 20 AAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGADGVEIHGAVGYLAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 112 RTIGLIRDH-----GCKAGLVLNPATPLSWLDHTLDKLDLVLLMSVNPGFGGQAFIPGVLDKVRQARARIDRQVAAGGrp 186
Cdd:cd04722 100 EDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGG-- 177
|
170 180
....*....|....*....|....*....
gi 1618902835 187 vwleidGGVKADNITEIARAGADTFVAGS 215
Cdd:cd04722 178 ------GINDPEDAAEALALGADGVIVGS 200
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
166-237 |
1.86e-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: 41.32 E-value: 1.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1618902835 166 LDKVRQARARIDRQVAAggrpvwleIdGGVKADNITEIARAGADTFVAGSAVFGAPDADGGYRGILHRLREA 237
Cdd:COG0352 144 LEGLAWWAELVEIPVVA--------I-GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
166-222 |
1.47e-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: 38.65 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1618902835 166 LDKVRQARARIDRQVAAggrpvwleIdGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:cd00564 139 LELLREIAELVEIPVVA--------I-GGITPENAAEVLAAGADGVAVISAITGADD 186
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
166-224 |
3.40e-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: 37.66 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 166 LDKVR-QARARIDRQVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAgSAVFGAPDAD 224
Cdd:cd01573 209 LDKFSpEELAELVPKLRSLAPPVLLAAAGGINIENAAAYAAAGADILVT-SAPYYAKPAD 267
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
163-222 |
4.21e-03 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 37.08 E-value: 4.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618902835 163 PGVLDKVRQARARIdrqvaaGGRPvWLEIdGGVKADNITEIARAGADTFVAGSAVFGAPD 222
Cdd:PRK00043 145 PQGLEGLREIRAAV------GDIP-IVAI-GGITPENAPEVLEAGADGVAVVSAITGAED 196
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
161-228 |
9.34e-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: 9.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1618902835 161 FIPGVLDKVRQARARIDRQVAAGGRPVWLEIDGGVKADNITEIARAGADTFVAGSAVFGAPDADGGYR 228
Cdd:cd00516 214 GSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAPPLDIVLK 281
|
|
| |
