|
Name |
Accession |
Description |
Interval |
E-value |
| UlaD |
COG0269 |
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]; |
1-209 |
3.25e-94 |
|
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
Pssm-ID: 440039 Cd Length: 212 Bit Score: 273.58 E-value: 3.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADY 80
Cdd:COG0269 4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 81 CTVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVeHS 160
Cdd:COG0269 84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKELV-GV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496558468 161 IVSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:COG0269 163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
|
|
| RuMP_HxlA |
TIGR03128 |
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ... |
2-207 |
4.95e-89 |
|
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.
Pssm-ID: 132172 [Multi-domain] Cd Length: 206 Bit Score: 260.38 E-value: 4.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 2 KLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYC 81
Cdd:TIGR03128 1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 82 TVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVEHSI 161
Cdd:TIGR03128 81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496558468 162 VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAI 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
1-203 |
1.07e-75 |
|
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: 226.31 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADY 80
Cdd:cd04726 1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 81 CTVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKeIEAVGVDFIGVHVGVDQQAVG-ITPLEKLAEMKSCVEh 159
Cdd:cd04726 81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKLLG- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496558468 160 SIVSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
3-209 |
3.97e-58 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 188.69 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDK-VHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYC 81
Cdd:PRK07028 6 LQVALDLLELDRAVEIAKEaVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 82 TVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVeHSI 161
Cdd:PRK07028 86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELLKEVSEEV-SIP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496558468 162 VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:PRK07028 165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDS 212
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
2-203 |
6.59e-37 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 127.67 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 2 KLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYpDCEILADTKIMDAGEYE---AEETFKAGA 78
Cdd:smart00934 1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVaraARAAAELGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 79 DYCTVLGVTDTLTIEGCVKAAKEYGK------------QTMVDMICVEDVPKRVKEI--EAVGVDFIGVHVGVDQQAvgi 144
Cdd:smart00934 80 DAVTVHAYAGSDMIEAALEAAKKYGPgllavtvltspgAEDLQELGDESLEEQVLRLakLAKEAGLDGVVCSATEPE--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558468 145 tpleklAEMKSCVEHSIVSVAG-GINLKTIEEY--KKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:smart00934 157 ------LIRRALGPDFLILTPGiGDQGRVATPAvaIGAGADIIVVGRPITQAADPVEAAEAI 212
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
1-203 |
2.76e-35 |
|
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: 123.91 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYpdCEILADTKIMDAGEYE---AEETFKAG 77
Cdd:pfam00215 1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHG--FLIFLDLKFADIGNTVakqAKYKAKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 78 ADYCTVLGVTDTLTIEGCVKAAKEYG-KQTMVDMICVEDvPKRVKEIEAVGVDFIGVHVGVDQQA--VGITPLEKLAEMK 154
Cdd:pfam00215 79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKG-SLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALRE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496558468 155 SCVEHSIV--------SVAGGINLKTIEEYKKLN-PEVIIVGGGINHAEDPVAAAKAI 203
Cdd:pfam00215 158 ILPDFLILtpgiglqgGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UlaD |
COG0269 |
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism]; |
1-209 |
3.25e-94 |
|
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
Pssm-ID: 440039 Cd Length: 212 Bit Score: 273.58 E-value: 3.25e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADY 80
Cdd:COG0269 4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 81 CTVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVeHS 160
Cdd:COG0269 84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKELV-GV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496558468 161 IVSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:COG0269 163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
|
|
| RuMP_HxlA |
TIGR03128 |
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ... |
2-207 |
4.95e-89 |
|
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate synthase (HPS), or the HPS domain of a fusion protein. This enzyme is part of the ribulose monophosphate (RuMP) pathway, which in one direction removes the toxic metabolite formaldehyde by assimilation into fructose-6-phosphate. In the other direction, in species lacking a complete pentose phosphate pathway, the RuMP pathway yields ribulose-5-phosphate, necessary for nucleotide biosynthesis, at the cost of also yielding formaldehyde. These latter species tend usually have a formaldehyde-activating enzyme to attach formaldehyde to the C1 carrier tetrahydromethanopterin. In these species, the enzyme is viewed as a lyase rather than a synthase and is called D-arabino 3-hexulose 6-phosphate formaldehyde lyase. Note that there is some overlap in specificity with the Escherichia coli enzyme 3-keto-L-gulonate 6-phosphate decarboxylase.
Pssm-ID: 132172 [Multi-domain] Cd Length: 206 Bit Score: 260.38 E-value: 4.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 2 KLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYC 81
Cdd:TIGR03128 1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 82 TVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVEHSI 161
Cdd:TIGR03128 81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496558468 162 VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAI 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
1-203 |
1.07e-75 |
|
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: 226.31 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADY 80
Cdd:cd04726 1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 81 CTVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKeIEAVGVDFIGVHVGVDQQAVG-ITPLEKLAEMKSCVEh 159
Cdd:cd04726 81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKLLG- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 496558468 160 SIVSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| PRK07028 |
PRK07028 |
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated |
3-209 |
3.97e-58 |
|
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
Pssm-ID: 235912 [Multi-domain] Cd Length: 430 Bit Score: 188.69 E-value: 3.97e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDK-VHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYC 81
Cdd:PRK07028 6 LQVALDLLELDRAVEIAKEaVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 82 TVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEAVGVDFIGVHVGVDQQAVGITPLEKLAEMKSCVeHSI 161
Cdd:PRK07028 86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELLKEVSEEV-SIP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 496558468 162 VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:PRK07028 165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDS 212
|
|
| ulaD |
PRK13306 |
3-dehydro-L-gulonate-6-phosphate decarboxylase; |
3-209 |
5.39e-40 |
|
3-dehydro-L-gulonate-6-phosphate decarboxylase;
Pssm-ID: 237344 Cd Length: 216 Bit Score: 135.83 E-value: 5.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYCT 82
Cdd:PRK13306 6 LQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAGADWVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 83 VLGVTDTLTIEGCVKAAKEYGKQTMVDMI---CVEDvpkrVKEIEAVGVDFIGVHVGVDQQAVGITPLEK-LAEMKSCVE 158
Cdd:PRK13306 86 VICAAHIPTIKAALKVAKEFNGEIQIELYgnwTWEQ----AQQWRDAGISQVIYHRSRDAQLAGVAWGEKdLNKVKKLSD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 496558468 159 HSI-VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:PRK13306 162 MGFkVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAFKDEIAK 213
|
|
| OMPdecase |
smart00934 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ... |
2-203 |
6.59e-37 |
|
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase (OMPdecase) catalyzes the last step in the de novo biosynthesis of pyrimidines, the decarboxylation of OMP into UMP. In higher eukaryotes OMPdecase is part, with orotate phosphoribosyltransferase, of a bifunctional enzyme, while the prokaryotic and fungal OMPdecases are monofunctional protein.
Pssm-ID: 214921 Cd Length: 212 Bit Score: 127.67 E-value: 6.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 2 KLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYpDCEILADTKIMDAGEYE---AEETFKAGA 78
Cdd:smart00934 1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVaraARAAAELGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 79 DYCTVLGVTDTLTIEGCVKAAKEYGK------------QTMVDMICVEDVPKRVKEI--EAVGVDFIGVHVGVDQQAvgi 144
Cdd:smart00934 80 DAVTVHAYAGSDMIEAALEAAKKYGPgllavtvltspgAEDLQELGDESLEEQVLRLakLAKEAGLDGVVCSATEPE--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558468 145 tpleklAEMKSCVEHSIVSVAG-GINLKTIEEY--KKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:smart00934 157 ------LIRRALGPDFLILTPGiGDQGRVATPAvaIGAGADIIVVGRPITQAADPVEAAEAI 212
|
|
| OMPdecase |
pfam00215 |
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ... |
1-203 |
2.76e-35 |
|
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: 123.91 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 1 MKLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYpdCEILADTKIMDAGEYE---AEETFKAG 77
Cdd:pfam00215 1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKHG--FLIFLDLKFADIGNTVakqAKYKAKLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 78 ADYCTVLGVTDTLTIEGCVKAAKEYG-KQTMVDMICVEDvPKRVKEIEAVGVDFIGVHVGVDQQA--VGITPLEKLAEMK 154
Cdd:pfam00215 79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKG-SLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALRE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 496558468 155 SCVEHSIV--------SVAGGINLKTIEEYKKLN-PEVIIVGGGINHAEDPVAAAKAI 203
Cdd:pfam00215 158 ILPDFLILtpgiglqgGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
|
|
| sgbH |
PRK13305 |
3-keto-L-gulonate-6-phosphate decarboxylase UlaD; |
3-208 |
1.39e-28 |
|
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
Pssm-ID: 183962 Cd Length: 218 Bit Score: 106.44 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGADYCT 82
Cdd:PRK13305 6 LQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANWMT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 83 VLGVTDTLTIEGCVKAAKEYGKQTMVDMI---CVEDvpkrVKEIEAVGVDFIGVHVGVDQQAVGIT-PLEKLAEMKSCVE 158
Cdd:PRK13305 86 IICAAPLATVEKGHAVAQRCGGEIQIELFgnwTLDD----ARDWHRIGVRQAIYHRGRDAQASGQQwGEADLARMKALSD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496558468 159 HSI-VSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAIN 208
Cdd:PRK13305 162 IGLeLSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQID 212
|
|
| PRK13307 |
PRK13307 |
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase; |
3-209 |
1.94e-22 |
|
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
Pssm-ID: 183964 [Multi-domain] Cd Length: 391 Bit Score: 93.54 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDKV----HTyvdIIEVGSPFIIEEGMRPVRIFKEKYPDCEILADTKIMDAGEYEAEETFKAGA 78
Cdd:PRK13307 175 LQVALDLPDLEEVERVLSQLpksdHI---IIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 79 DYCTVLGVTDTLTIEGCVKAAKEYGKQTMVDMICVEDVPKRVKEIEaVGVDFIGVHVGVDQQAVGiTPLEKLAEMKSCVE 158
Cdd:PRK13307 252 DAVVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLK-VKPDVVELHRGIDEEGTE-HAWGNIKEIKKAGG 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 496558468 159 HSIVSVAGGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAINQ 209
Cdd:PRK13307 330 KILVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDFLNKLKP 380
|
|
| pyrF |
TIGR01740 |
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ... |
3-203 |
3.93e-13 |
|
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5'-monophosphate decarboxylase, the PyrF protein of pyrimidine nucleotide biosynthesis. In many eukaryotes, the region hit by this model is part of a multifunctional protein. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273785 Cd Length: 214 Bit Score: 65.45 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 3 LQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKypDCEILADTKIMDAG---EYEAEETFKAGAD 79
Cdd:TIGR01740 1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKL--NKLIFLDLKFADIPntvKLQYESKIKLGAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 80 YCTVLGVTDTLTIEGCVKAAKEYGKQ---------TMVDMICVEDVPKRVKEIEAVGVDFigvhvGVDqqavGITPLEKL 150
Cdd:TIGR01740 79 MVNVHGFAGSESVEAAKEAASEFGRRgllavteltSMGSEEYGEDTMEKVVEYAKEAKEF-----GLI----GPVCSAEE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496558468 151 AEMKSCVEHSIVSVAGGINLK-----------TIEEYKKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:TIGR01740 150 AKEIRKATGDFLILTPGIRLDskdaddqkrvvTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRI 213
|
|
| PRK13813 |
PRK13813 |
orotidine 5'-phosphate decarboxylase; Provisional |
2-208 |
5.16e-13 |
|
orotidine 5'-phosphate decarboxylase; Provisional
Pssm-ID: 237520 Cd Length: 215 Bit Score: 65.00 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 2 KLQLALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYPdceILADTKIMD---AGEYEAEETFKAGA 78
Cdd:PRK13813 5 RIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADipnTNRLICEAVFEAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 79 DYCTVLGVTDTLTIEGCVKAAKEYGKQTMVdmicvedvpkrVKEIEAVGV-DFIGVHV----------GVDQQAVGITPL 147
Cdd:PRK13813 82 WGIIVHGFTGRDSLKAVVEAAAESGGKVFV-----------VVEMSHPGAlEFIQPHAdklaklaqeaGAFGVVAPATRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496558468 148 EKLAEMKSCVEHSIVSVAGGINLKTIEEYKKLN--PEVIIVGGGINHAEDPVAAAKAIYEAIN 208
Cdd:PRK13813 151 ERVRYIRSRLGDELKIISPGIGAQGGKAADAIKagADYVIVGRSIYNAADPREAAKAINEEIR 213
|
|
| OMP_decarboxylase_like |
cd04725 |
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ... |
5-203 |
4.26e-11 |
|
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.
Pssm-ID: 240076 Cd Length: 216 Bit Score: 59.88 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 5 LALDDITLDDAVELLDKVHTYVDIIEVGSPFIIEEGMRPVRIFKEKYpdCEILADTKIMDAG---EYEAEETFKAGADYC 81
Cdd:cd04725 3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG--FLVFLDLKLGDIPntvAAAAEALLGLGADAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 82 TVLGVTDTLTIEGCVKAAKEYGK----------------QTMVDMICVEDVPKRVKEIEAVGVDfiGVHVGvdqqavgit 145
Cdd:cd04725 81 TVHPYGGSDMLKAALEAAEEKGKglfavtvlsspgaldlQEGIPGSLEDLVERLAKLAREAGVD--GVVCG--------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496558468 146 PLEKLAEMKSCVEHSIVsVAGGINLK----------TIEEYKKLNPEVIIVGGGINHAEDPVAAAKAI 203
Cdd:cd04725 150 ATEPEALRRALGPDFLI-LTPGIGAQgsgddqkrggTPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
120-205 |
2.89e-03 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 37.11 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496558468 120 VKEIEAVGVDFIGV-HVG------VDQQAVGITPLEKLAEMkscveHSIVSVA-GGINLKTIEEYKKLNPEVIIVGGGIN 191
Cdd:cd00564 108 ALRAEELGADYVGFgPVFptptkpGAGPPLGLELLREIAEL-----VEIPVVAiGGITPENAAEVLAAGADGVAVISAIT 182
|
90
....*....|....
gi 496558468 192 HAEDPVAAAKAIYE 205
Cdd:cd00564 183 GADDPAAAARELLA 196
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
147-207 |
5.86e-03 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 36.54 E-value: 5.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496558468 147 LEKLAEMKSCVehSIVSVA-GGINLKTIEEYKKLNPEVIIVGGGINHAEDPVAAAKAIYEAI 207
Cdd:PRK07695 138 LEELSDIARAL--SIPVIAiGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRYAESI 197
|
|
| |
