|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-225 |
8.44e-139 |
|
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: 387.51 E-value: 8.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 4 YRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 84 GASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAM 163
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488161283 164 LDryeaQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAKA 225
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-219 |
5.35e-133 |
|
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: 372.38 E-value: 5.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 6 IAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAGA 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 86 SIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLD 165
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488161283 166 RYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMR 219
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-224 |
1.53e-129 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 364.12 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 1 MTTYRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSF 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 81 AKAGASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRV 160
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488161283 161 RAMLDRYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAK 224
Cdd:PRK05581 161 RKLIDER----GLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-219 |
9.21e-126 |
|
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: 354.09 E-value: 9.21e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 6 IAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAGA 85
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 86 SIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLD 165
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488161283 166 ryeaQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMR 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 |
7.68e-109 |
|
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: 310.80 E-value: 7.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 5 RIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAG 84
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 85 ASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAML 164
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488161283 165 DRYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIF 206
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rpe |
COG0036 |
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ... |
4-225 |
8.44e-139 |
|
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: 387.51 E-value: 8.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 4 YRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKA 83
Cdd:COG0036 1 IKIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 84 GASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAM 163
Cdd:COG0036 81 GADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488161283 164 LDryeaQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAKA 225
Cdd:COG0036 161 ID----ERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALREAAAAA 218
|
|
| rpe |
TIGR01163 |
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ... |
6-219 |
5.35e-133 |
|
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: 372.38 E-value: 5.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 6 IAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAGA 85
Cdd:TIGR01163 1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 86 SIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLD 165
Cdd:TIGR01163 81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488161283 166 RYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMR 219
Cdd:TIGR01163 161 EL----GLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
|
|
| PRK05581 |
PRK05581 |
ribulose-phosphate 3-epimerase; Validated |
1-224 |
1.53e-129 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 235515 Cd Length: 220 Bit Score: 364.12 E-value: 1.53e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 1 MTTYRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSF 80
Cdd:PRK05581 1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 81 AKAGASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRV 160
Cdd:PRK05581 81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488161283 161 RAMLDRYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAK 224
Cdd:PRK05581 161 RKLIDER----GLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRAELAA 220
|
|
| RPE |
cd00429 |
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ... |
6-219 |
9.21e-126 |
|
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: 354.09 E-value: 9.21e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 6 IAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAGA 85
Cdd:cd00429 2 IAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 86 SIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLD 165
Cdd:cd00429 82 DIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELIP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488161283 166 ryeaQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMR 219
Cdd:cd00429 162 ----ENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
|
|
| PLN02334 |
PLN02334 |
ribulose-phosphate 3-epimerase |
1-226 |
1.10e-110 |
|
ribulose-phosphate 3-epimerase
Pssm-ID: 215192 Cd Length: 229 Bit Score: 316.94 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 1 MTTYRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSF 80
Cdd:PLN02334 5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 81 AKAGASIITFHPEASR--HIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLD--RLDMVLLMSVNPGFGGQSFIPHTLEK 156
Cdd:PLN02334 85 AKAGASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVEkgLVDMVLVMSVEPGFGGQSFIPSMMDK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 157 IRRVRAMLDRyeaqsgrhITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAKAA 226
Cdd:PLN02334 165 VRALRKKYPE--------LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRASVEKAA 226
|
|
| Ribul_P_3_epim |
pfam00834 |
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ... |
5-206 |
7.68e-109 |
|
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: 310.80 E-value: 7.68e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 5 RIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAG 84
Cdd:pfam00834 1 KIAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 85 ASIITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAML 164
Cdd:pfam00834 81 ADIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488161283 165 DRYeaqsGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIF 206
Cdd:pfam00834 161 DER----GLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
|
|
| PTZ00170 |
PTZ00170 |
D-ribulose-5-phosphate 3-epimerase; Provisional |
6-224 |
4.22e-77 |
|
D-ribulose-5-phosphate 3-epimerase; Provisional
Pssm-ID: 240303 Cd Length: 228 Bit Score: 231.80 E-value: 4.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 6 IAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPY-ASVPIDVHLMVEPVDDLIQSFAKAG 84
Cdd:PTZ00170 9 IAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHlPNTFLDCHLMVSNPEKWVDDFAKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 85 ASIITFHPEA-SRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDR--LDMVLLMSVNPGFGGQSFIPHTLEKIRRVR 161
Cdd:PTZ00170 89 ASQFTFHIEAtEDDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRELR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488161283 162 AmldRYEaqsgrHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAK 224
Cdd:PTZ00170 169 K---RYP-----HLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRESVQK 223
|
|
| PRK09722 |
PRK09722 |
allulose-6-phosphate 3-epimerase; Provisional |
3-207 |
2.17e-66 |
|
allulose-6-phosphate 3-epimerase; Provisional
Pssm-ID: 236616 Cd Length: 229 Bit Score: 204.46 E-value: 2.17e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 3 TYRIAPSILSADFARLGEEVEsVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAK 82
Cdd:PRK09722 2 RMKISPSLMCMDLLKFKEQIE-FLNSKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 83 AGASIITFHPE-ASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVR 161
Cdd:PRK09722 81 AGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAELK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488161283 162 amldRYEAQSGRHITIEVDGGIKTDNIAAVARAGADTFVAG-SAIFG 207
Cdd:PRK09722 161 ----ALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGtSGLFN 203
|
|
| PRK08005 |
PRK08005 |
ribulose-phosphate 3 epimerase family protein; |
8-215 |
3.32e-30 |
|
ribulose-phosphate 3 epimerase family protein;
Pssm-ID: 169179 Cd Length: 210 Bit Score: 111.28 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 8 PSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEPVDDLIQSFAKAGASI 87
Cdd:PRK08005 5 PSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIRPGW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 88 ITFHPEASRHIDRSLSLIRDMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLDRY 167
Cdd:PRK08005 85 IFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHFPAA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488161283 168 EAQSgrhitievDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVI 215
Cdd:PRK08005 165 ECWA--------DGGITLRAARLLAAAGAQHLVIGRALFTTANYDVTL 204
|
|
| PRK08091 |
PRK08091 |
ribulose-phosphate 3-epimerase; Validated |
1-213 |
1.81e-22 |
|
ribulose-phosphate 3-epimerase; Validated
Pssm-ID: 169215 Cd Length: 228 Bit Score: 91.48 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 1 MTTYRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMvcaALKPYASVPI-DVHLMVEPVDDLIQS 79
Cdd:PRK08091 10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAI---AIKQFPTHCFkDVHLMVRDQFEVAKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 80 FAKAGASIITFHPEASRHIDRSLSLIR----DMGCqaGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLE 155
Cdd:PRK08091 87 CVAAGADIVTLQVEQTHDLALTIEWLAkqktTVLI--GLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488161283 156 KIRRVRAMLdryeAQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKA 213
Cdd:PRK08091 165 RVIQVENRL----GNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKT 218
|
|
| PRK14057 |
PRK14057 |
epimerase; Provisional |
1-206 |
4.71e-21 |
|
epimerase; Provisional
Pssm-ID: 172549 Cd Length: 254 Bit Score: 88.20 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 1 MTTYRIAPSILSADFARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALkPYASVPiDVHLMVEPVDDLIQSF 80
Cdd:PRK14057 17 LASYPLSVGILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVGPWAVGQL-PQTFIK-DVHLMVADQWTAAQAC 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 81 AKAGASIITFHPEASRHIDRSLSLIR---------DMGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIP 151
Cdd:PRK14057 95 VKAGAHCITLQAEGDIHLHHTLSWLGqqtvpviggEMPVIRGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488161283 152 HTLEKIRRVRAML-DRYEAQsgrhiTIEVDGGIKTDNIAAVARAGADTFVAGSAIF 206
Cdd:PRK14057 175 DLHERVAQLLCLLgDKREGK-----IIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
16-203 |
1.15e-07 |
|
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: 50.28 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 16 ARLGEEVESVIAAGADLIHFDVMDNHYVPNLTFGPMVCAALKPYASVPIDVHLMVEP----VDDLIQSFAKAGASIITFH 91
Cdd:cd04722 12 GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDaaaaVDIAAAAARAAGADGVEIH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488161283 92 PEASRHIDRSLSLIRD-----MGCQAGLVLNPATPVYLLENVLDRLDMVLLMSVNPGFGGQSFIPHTLEKIRRVRAMLDr 166
Cdd:cd04722 92 GAVGYLAREDLELIRElreavPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSK- 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 488161283 167 yeaqsgrhITIEVDGGIKTDNIAAVARA-GADTFVAGS 203
Cdd:cd04722 171 --------VPVIAGGGINDPEDAAEALAlGADGVIVGS 200
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
181-219 |
2.26e-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: 43.66 E-value: 2.26e-05
10 20 30
....*....|....*....|....*....|....*....
gi 488161283 181 GGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMR 219
Cdd:cd00564 157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
181-225 |
4.28e-05 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 42.86 E-value: 4.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488161283 181 GGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAKA 225
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAALEAA 206
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
151-226 |
1.09e-04 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 41.71 E-value: 1.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488161283 151 PHTLEKIRRVRAmldryeaqSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAMRVELAKAA 226
Cdd:PRK00043 145 PQGLEGLREIRA--------AVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAFRAAR 212
|
|
| PRTase_typeII |
cd00516 |
Phosphoribosyltransferase (PRTase) type II; This family contains two enzymes that play an ... |
148-209 |
2.48e-04 |
|
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: 41.07 E-value: 2.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488161283 148 SFIPHTLEKIRRVRAMLDRYEAQSGRHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKP 209
Cdd:cd00516 213 SGSPEELDPAVLILKARAHLDGKGLPRVKIEASGGLDEENIRAYAETGVDVFGVGTLLHSAP 274
|
|
| modD_like |
cd01573 |
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ... |
174-215 |
1.28e-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: 38.82 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488161283 174 HITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKP-DYKAVI 215
Cdd:cd01573 230 PVLLAAAGGINIENAAAYAAAGADILVTSAPYYAKPaDIKVKI 272
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
174-218 |
2.73e-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: 37.56 E-value: 2.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488161283 174 HITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKPDYKAVIDAM 218
Cdd:cd04726 158 GVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| QPRTase_NadC |
cd01568 |
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
153-209 |
7.89e-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: 36.68 E-value: 7.89e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488161283 153 TLEKIRRVRAMLDRYEaqsgrHITIEVDGGIKTDNIAAVARAGADTFVAGSAIFGKP 209
Cdd:cd01568 211 SPEELKEAVKLLKGLP-----RVLLEASGGITLENIRAYAETGVDVISTGALTHSAP 262
|
|
| |
