|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-224 |
1.28e-134 |
|
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439806 Cd Length: 218 Bit Score: 376.72 E-value: 1.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 4 FRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 84 GANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKR 163
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654743505 164 IDaykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALAN 224
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAA 217
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-224 |
1.17e-131 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 369.51 E-value: 1.17e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 1 MTQFRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDF 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 81 AKAGANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREA 160
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654743505 161 RKRIDaykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALAN 224
Cdd:PRK05581 161 RKLID----ERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-219 |
1.39e-125 |
|
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: 353.89 E-value: 1.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGA 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 86 NLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRID 165
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 166 AYkektGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMR 219
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-219 |
1.73e-121 |
|
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: 343.31 E-value: 1.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGA 85
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 86 NLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRID 165
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 166 aykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMR 219
Cdd:cd00429 162 ----ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
5-206 |
9.34e-114 |
|
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: 323.51 E-value: 9.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 5 RIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAG 84
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 85 ANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRI 164
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 654743505 165 DAYkektGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIF 206
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-224 |
1.28e-134 |
|
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439806 Cd Length: 218 Bit Score: 376.72 E-value: 1.28e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 4 FRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 84 GANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKR 163
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654743505 164 IDaykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALAN 224
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAA 217
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-224 |
1.17e-131 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 369.51 E-value: 1.17e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 1 MTQFRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDF 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 81 AKAGANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREA 160
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654743505 161 RKRIDaykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALAN 224
Cdd:PRK05581 161 RKLID----ERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-219 |
1.39e-125 |
|
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: 353.89 E-value: 1.39e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGA 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 86 NLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRID 165
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 166 AYkektGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMR 219
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-219 |
1.73e-121 |
|
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: 343.31 E-value: 1.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGA 85
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 86 NLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRID 165
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 166 aykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMR 219
Cdd:cd00429 162 ----ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
5-224 |
2.16e-115 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 328.88 E-value: 2.16e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 5 RIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAG 84
Cdd:PLN02334 9 IIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 85 ANLISFHPEGS--DHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDK--VDLVLIMSVNPGFGGQSFIPEALVKLREA 160
Cdd:PLN02334 89 ASIFTFHIEQAstIHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEKglVDMVLVMSVEPGFGGQSFIPSMMDKVRAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654743505 161 RKRIDaykektgrEIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALAN 224
Cdd:PLN02334 169 RKKYP--------ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEK 224
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
5-206 |
9.34e-114 |
|
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: 323.51 E-value: 9.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 5 RIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAG 84
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 85 ANLISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRI 164
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 654743505 165 DAYkektGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIF 206
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
6-221 |
4.09e-76 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 229.10 E-value: 4.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHV-DVPIDVHLMVRPVDRIVPDFAKAG 84
Cdd:PTZ00170 9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLpNTFLDCHLMVSNPEKWVDDFAKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 85 ANLISFHPEG-SDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDK--VDLVLIMSVNPGFGGQSFIPEALVKLREAR 161
Cdd:PTZ00170 89 ASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRELR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 162 KRidaYKektgrEIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAA 221
Cdd:PTZ00170 169 KR---YP-----HLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRES 220
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
6-210 |
9.55e-64 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 197.91 E-value: 9.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 6 IAPSILSADFARLGEEVRnVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGA 85
Cdd:PRK09722 5 ISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLADAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 86 NLISFHPEG-SDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARkri 164
Cdd:PRK09722 84 DFITLHPETiNGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELK--- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 654743505 165 dAYKEKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAG-SAIFGAPD 210
Cdd:PRK09722 161 -ALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFNLDE 206
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
8-220 |
1.44e-31 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 114.75 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 8 PSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAKAGANL 87
Cdd:PRK08005 5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 88 ISFHPEGSDHIDRTLSLIRDHGCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRIDAY 167
Cdd:PRK08005 85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFPAA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 654743505 168 KektgreihLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRA 220
Cdd:PRK08005 165 E--------CWADGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTLSQFTA 209
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
1-222 |
1.20e-17 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 78.38 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 1 MTQFRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVpiDVHLMVRPVDRIVPDF 80
Cdd:PRK08091 10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK--DVHLMVRDQFEVAKAC 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 81 AKAGANLISFHPEGSDHIDRTLSLIRDHGCKA--GLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLR 158
Cdd:PRK08091 88 VAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654743505 159 EARKRIDaykeKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAAL 222
Cdd:PRK08091 168 QVENRLG----NRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKSSL 227
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
1-206 |
2.89e-15 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 72.41 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 1 MTQFRIAPSILSADFARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIrPHVDVPiDVHLMVRPVDRIVPDF 80
Cdd:PRK14057 17 LASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 81 AKAGANLISFHPEGSDHIDRTLSLIRDHGCKA---------GLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQsfIP 151
Cdd:PRK14057 95 VKAGAHCITLQAEGDIHLHHTLSWLGQQTVPViggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSK--MR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 654743505 152 EALVKLREARKRIDAYKEKTGREIhlEVDGGVKVDNIAEIAAAGADTFVAGSAIF 206
Cdd:PRK14057 173 SSDLHERVAQLLCLLGDKREGKII--VIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
16-203 |
3.73e-08 |
|
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: 51.82 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 16 ARLGEEVRNVVAAGADWIHFDVMDNHYVPNLTIGPLVCEAIRPHVDVPIDVHLMVRPVDRIVPDFAK----AGANLISFH 91
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGADGVEIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 92 PEGSDHIDRTLSLIRDH-----GCKAGLVFNPATSLNHLDYVMDKVDLVLIMSVNPGFGGQSFIPEALVKLREARKRIDa 166
Cdd:cd04722 92 GAVGYLAREDLELIRELreavpDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK- 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 654743505 167 ykektgreIHLEVDGGVKV-DNIAEIAAAGADTFVAGS 203
Cdd:cd04722 171 --------VPVIAGGGINDpEDAAEALALGADGVIVGS 200
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
181-223 |
6.18e-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: 45.56 E-value: 6.18e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 654743505 181 GGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALA 223
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALE 204
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
181-220 |
1.02e-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: 44.82 E-value: 1.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 654743505 181 GGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRA 220
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
165-218 |
2.65e-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: 43.34 E-value: 2.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 165 DAYKEKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKM 218
Cdd:cd04726 149 DLKKVKKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
154-223 |
8.81e-05 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 42.09 E-value: 8.81e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654743505 154 LVKLREARKRIdaykektgREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAALA 223
Cdd:PRK00043 148 LEGLREIRAAV--------GDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFR 209
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
148-209 |
1.08e-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: 39.15 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654743505 148 SFIPEALVKLREARKRIDAYKEKTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAP 209
Cdd:cd00516 213 SGSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAP 274
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
157-209 |
1.41e-03 |
|
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; Nicotinate-nucleotide pyrophosphorylase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 439927 [Multi-domain] Cd Length: 272 Bit Score: 38.85 E-value: 1.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 654743505 157 LREARKRIDaykektGReIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAP 209
Cdd:COG0157 217 LREAVALLR------GR-ALLEASGGITLENIRAYAETGVDYISVGALTHSAP 262
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
156-209 |
1.64e-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: 38.06 E-value: 1.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 654743505 156 KLREARKRIDAykekTGREIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAP 209
Cdd:pfam01729 113 EVKKAVEELDE----RNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVP 162
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
164-222 |
2.51e-03 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 38.45 E-value: 2.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 654743505 164 IDAYKEKTGReIHLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAPDHKAVIDKMRAAL 222
Cdd:PRK13307 321 IKEIKKAGGK-ILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKL 378
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
157-209 |
2.70e-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: 37.84 E-value: 2.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 654743505 157 LREARKRIDAYKEKTgreihLEVDGGVKVDNIAEIAAAGADTFVAGSAIFGAP 209
Cdd:cd01568 215 LKEAVKLLKGLPRVL-----LEASGGITLENIRAYAETGVDVISTGALTHSAP 262
|
|
| |
