|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
3-216 |
6.90e-126 |
|
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: 354.38 E-value: 6.90e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 3 PIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKAL 82
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 83 GAHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRAL 162
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490442102 163 IERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHEL 216
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
4-214 |
1.83e-110 |
|
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: 315.19 E-value: 1.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 4 IIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALG 83
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 84 AHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALI 163
Cdd:cd00429 81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490442102 164 ERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLH 214
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-213 |
7.46e-108 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 308.65 E-value: 7.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 1 MKPIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVK 80
Cdd:PRK05581 2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 81 ALGAHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELR 160
Cdd:PRK05581 82 KAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490442102 161 ALIERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQL 213
Cdd:PRK05581 162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSL 214
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
5-214 |
2.52e-97 |
|
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: 281.86 E-value: 2.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 5 IAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALGA 84
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 85 HTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALIE 164
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490442102 165 RTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLH 214
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
4-201 |
2.14e-85 |
|
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: 251.10 E-value: 2.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 4 IIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALG 83
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 84 AHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALI 163
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 490442102 164 ERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVF 201
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
3-216 |
6.90e-126 |
|
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: 354.38 E-value: 6.90e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 3 PIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKAL 82
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 83 GAHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRAL 162
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490442102 163 IERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHEL 216
Cdd:COG0036 161 IDERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREA 214
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
4-214 |
1.83e-110 |
|
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: 315.19 E-value: 1.83e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 4 IIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALG 83
Cdd:cd00429 1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 84 AHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALI 163
Cdd:cd00429 81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490442102 164 ERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLH 214
Cdd:cd00429 161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-213 |
7.46e-108 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 308.65 E-value: 7.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 1 MKPIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVK 80
Cdd:PRK05581 2 KMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 81 ALGAHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELR 160
Cdd:PRK05581 82 KAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIRELR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490442102 161 ALIERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQL 213
Cdd:PRK05581 162 KLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSL 214
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
5-214 |
2.52e-97 |
|
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: 281.86 E-value: 2.52e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 5 IAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALGA 84
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 85 HTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALIE 164
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490442102 165 RTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLH 214
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
4-201 |
2.14e-85 |
|
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: 251.10 E-value: 2.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 4 IIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALG 83
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 84 AHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALI 163
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 490442102 164 ERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVF 201
Cdd:pfam00834 161 DERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
3-213 |
1.95e-84 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 249.92 E-value: 1.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 3 PIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKAL 82
Cdd:PLN02334 8 AIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDFAKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 83 GAHTMNVHYEACP--HLHRVIQQIREAGMQPAVTINPATPVALLQDII--RDVYMVLIMSVNPGFGGQKFIEHSVEKVRE 158
Cdd:PLN02334 88 GASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVekGLVDMVLVMSVEPGFGGQSFIPSMMDKVRA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490442102 159 LRALIErtgsKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQL 213
Cdd:PLN02334 168 LRKKYP----ELDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGL 218
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
1-215 |
6.79e-77 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 230.64 E-value: 6.79e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 1 MKPIIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKP-LDVHLMIVNPEKFIPEV 79
Cdd:PTZ00170 5 LKAIIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNTfLDCHLMVSNPEKWVDDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 80 KALGAHTMNVHYEAC-PHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRD--VYMVLIMSVNPGFGGQKFIEHSVEKV 156
Cdd:PTZ00170 85 AKAGASQFTFHIEATeDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490442102 157 RELRalieRTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHE 215
Cdd:PTZ00170 165 RELR----KRYPHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRE 219
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
1-215 |
1.38e-57 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 181.73 E-value: 1.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 1 MKPIIAPSILSADFGYLAKDIEMVNrSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVK 80
Cdd:PRK09722 1 MRMKISPSLMCMDLLKFKEQIEFLN-SKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 81 ALGAHTMNVHYE-ACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVREL 159
Cdd:PRK09722 80 DAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490442102 160 RALIERTGSKALIEVDGGVNLETGARLVEAGADALVAGNA-VFGAQDPVE-----MIRQLHE 215
Cdd:PRK09722 160 KALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSgLFNLDEDIDeawdiMTAQIEA 221
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
4-205 |
2.91e-31 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 113.59 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 4 IIAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKPLDVHLMIVNPEKFIPEVKALG 83
Cdd:PRK08005 2 ILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 84 AHTMNVHYEACPHLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRALI 163
Cdd:PRK08005 82 PGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490442102 164 ERTGSKAlievDGGVNLETGARLVEAGADALVAGNAVFGAQD 205
Cdd:PRK08005 162 PAAECWA----DGGITLRAARLLAAAGAQHLVIGRALFTTAN 199
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
5-205 |
5.57e-20 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 84.54 E-value: 5.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 5 IAPSILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKplDVHLMIVNPEKFIPEVKALGA 84
Cdd:PRK08091 15 ISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK--DVHLMVRDQFEVAKACVAAGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 85 HTMNVHYEACPHLHRVIQQIRE--AGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVRELRAL 162
Cdd:PRK08091 93 DIVTLQVEQTHDLALTIEWLAKqkTTVLIGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVIQVENR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490442102 163 IERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQD 205
Cdd:PRK08091 173 LGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGE 215
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
9-211 |
3.03e-16 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 74.72 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 9 ILSADFGYLAKDIEMVNRSEAEWVHIDIMDGVFVPNISFGFPVLKYVAKLSKKplDVHLMIVNPEKFIPEVKALGAHTMN 88
Cdd:PRK14057 26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQLPQTFIK--DVHLMVADQWTAAQACVKAGAHCIT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 89 VHYEACPHLHRVIQQIRE------AGMQP---AVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQKFIEHSVEKVREL 159
Cdd:PRK14057 104 LQAEGDIHLHHTLSWLGQqtvpviGGEMPvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHERVAQL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490442102 160 RALIERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIR 211
Cdd:PRK14057 184 LCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALFRDDRLVENTR 235
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
176-215 |
9.84e-05 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 41.74 E-value: 9.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490442102 176 GGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHE 215
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
163-212 |
1.70e-04 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 41.54 E-value: 1.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 490442102 163 IERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQ 212
Cdd:PRK13307 324 IKKAGGKILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAED 373
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
176-216 |
2.01e-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: 40.94 E-value: 2.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490442102 176 GGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHEL 216
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAA 202
|
|
| NadC |
COG0157 |
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ... |
158-197 |
4.96e-04 |
|
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: 40.00 E-value: 4.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 490442102 158 ELRALIERTGSKALIEVDGGVNLETGARLVEAGADALVAG 197
Cdd:COG0157 216 ELREAVALLRGRALLEASGGITLENIRAYAETGVDYISVG 255
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
159-216 |
8.36e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 39.01 E-value: 8.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 490442102 159 LRALIERTGSKALIEVdGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQLHEL 216
Cdd:PRK00043 151 LREIRAAVGDIPIVAI-GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAA 207
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
9-213 |
1.31e-03 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5'-phosphate decarboxylase enzymes EC:4.1.1.23 that are involved in the final step of pyrimidine biosynthesis. The family also includes enzymes such as hexulose-6-phosphate synthase. This family appears to be distantly related to pfam00834.
Pssm-ID: 395160 Cd Length: 215 Bit Score: 38.40 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 9 ILSADFGYLAKDIEMVNR--SEAEW--VHIDIMdgvfvpnISFGFPVLKYVAKLSKKP-LDVHLM-IVNPEKFIPEVKA- 81
Cdd:pfam00215 4 CVALDVPTLEEALELADElgPYVDIlkVGTPLF-------EAFGLKLVAELRKHGFLIfLDLKFAdIGNTVAKQAKYKAk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 82 LGAHTMNVHyeACPHLhRVIQQIREAG-------MQPAVTINPaTPVALLQDIIRDVYMVLIM------SVNPGF--GGQ 146
Cdd:pfam00215 77 LGADIVTVH--AYAGE-GTLKAAKEAAeeygrglLLVAELSSK-GSLDLQEEGDLGYTQEIVHraadlaAGVDGVvaSAT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490442102 147 KFIEHSVEKVRELRALIERTGSKALievdGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQL 213
Cdd:pfam00215 153 EALREILPDFLILTPGIGLQGGDAG----GQQRVTTPAVAKEAGADIIIVGRGITGAGDPVAAARAI 215
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
168-213 |
1.68e-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: 37.95 E-value: 1.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 490442102 168 SKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQDPVEMIRQL 213
Cdd:cd04726 157 LGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| trpA |
PRK13125 |
tryptophan synthase subunit alpha; Provisional |
96-200 |
2.94e-03 |
|
tryptophan synthase subunit alpha; Provisional
Pssm-ID: 237286 Cd Length: 244 Bit Score: 37.71 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442102 96 HLHRVIQQIREAGMQPAVTINPATPVALLQDIIRDVYMVLIMSVNPGFGGQ--KFIEHSVEKVRELralierTGSKALIe 173
Cdd:PRK13125 117 DLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIYYGLRPATGVPlpVSVERNIKRVRNL------VGNKYLV- 189
|
90 100
....*....|....*....|....*...
gi 490442102 174 VDGGVN-LETGARLVEAGADALVAGNAV 200
Cdd:PRK13125 190 VGFGLDsPEDARDALSAGADGVVVGTAF 217
|
|
| QRPTase_C |
pfam01729 |
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
152-204 |
3.55e-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: 36.91 E-value: 3.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490442102 152 SVEKVRELRALIERTGSKALIEVDGGVNLETGARLVEAGADALVAGNAVFGAQ 204
Cdd:pfam01729 110 SPEEVKKAVEELDERNPRVLLEVSGGVTLDNVLEYAKTGVDVISVGALTHSVP 162
|
|
| |
