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Conserved domains on  [gi|16766067|ref|NP_461682|]
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putative hexulose 6 phosphate synthase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]

Protein Classification

3-hexulose-6-phosphate synthase( domain architecture ID 10022149)

3-hexulose-6-phosphate synthase catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 2-207 1.59e-101

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: 291.97  E-value: 1.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    82 TVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVRRKAR 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 16766067   162 IAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVL 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
 
Name Accession Description Interval E-value
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 2-207 1.59e-101

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: 291.97  E-value: 1.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    82 TVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVRRKAR 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 16766067   162 IAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVL 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-210 4.89e-84

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 440039  Cd Length: 212  Bit Score: 247.77  E-value: 4.89e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADY 80
Cdd:COG0269   4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  81 VTVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVrRKA 160
Cdd:COG0269  84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKEL-VGV 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16766067 161 RIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVLLQH 210
Cdd:COG0269 163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 1-203 6.64e-78

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: 232.09  E-value: 6.64e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADY 80
Cdd:cd04726   1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  81 VTVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDlPARVRLLEEAGADMLAVHTGTDQQAAG-RKPIDDLITMLKVrRK 159
Cdd:cd04726  81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVED-PEKRAKLLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKL-LG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16766067 160 ARIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 3-207 5.52e-51

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 170.20  E-value: 5.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    3 LQLALDELTLPEAMVFMDKVVDD-VDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYV 81
Cdd:PRK07028   6 LQVALDLLELDRAVEIAKEAVAGgADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   82 TVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIdDLITMLKVRRKAR 161
Cdd:PRK07028  86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPL-ELLKEVSEEVSIP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16766067  162 IAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVL 207
Cdd:PRK07028 165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAI 210
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 2-203 9.69e-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: 127.28  E-value: 9.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067      2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYpHKEVLADAKIMDGGHFESQL---LFDAGA 78
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVARAaraAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     79 DYVTVLGVTDVLTIQSCIRAAKEAG-KQVVVDM-----------ICVDDLPARVRLLEE--AGADMLAVHTGTDQQAAGR 144
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVltspgaedlqeLGDESLEEQVLRLAKlaKEAGLDGVVCSATEPELIR 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16766067    145 KPIDDlitmlkvrrKARIAVAGGISSQ---TVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:smart00934 160 RALGP---------DFLILTPGIGDQGrvaTPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 1-203 6.79e-33

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: 117.75  E-value: 6.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKypHKEVLADAKIMDGGHFESQ---LLFDAG 77
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKqakYKAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    78 ADYVTVLGVTDVLTIQSCIRAAKEAG-KQVVVDMICVDDLPARVRLLEEaGADMLAVHTGTDQQA-----------AGRK 145
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDL-GYTQEIVHRAADLAAgvdgvvasateALRE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   146 PIDDLITMLK-VRrkARIAVAGGISSQTVKDYALL-GPDVVIVGSAITHAADPAGEARKI 203
Cdd:pfam00215 158 ILPDFLILTPgIG--LQGGDAGGQQRVTTPAVAKEaGADIIIVGRGITGAGDPVAAARAI 215
 
Name Accession Description Interval E-value
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 2-207 1.59e-101

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: 291.97  E-value: 1.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    82 TVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVRRKAR 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 16766067   162 IAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVL 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-210 4.89e-84

3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];


Pssm-ID: 440039  Cd Length: 212  Bit Score: 247.77  E-value: 4.89e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADY 80
Cdd:COG0269   4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  81 VTVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVrRKA 160
Cdd:COG0269  84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKEL-VGV 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16766067 161 RIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVLLQH 210
Cdd:COG0269 163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 1-203 6.64e-78

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: 232.09  E-value: 6.64e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADY 80
Cdd:cd04726   1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  81 VTVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDlPARVRLLEEAGADMLAVHTGTDQQAAG-RKPIDDLITMLKVrRK 159
Cdd:cd04726  81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVED-PEKRAKLLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKL-LG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16766067 160 ARIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 3-207 5.52e-51

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 170.20  E-value: 5.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    3 LQLALDELTLPEAMVFMDKVVDD-VDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYV 81
Cdd:PRK07028   6 LQVALDLLELDRAVEIAKEAVAGgADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   82 TVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIdDLITMLKVRRKAR 161
Cdd:PRK07028  86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPL-ELLKEVSEEVSIP 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16766067  162 IAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQVL 207
Cdd:PRK07028 165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAI 210
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 2-203 9.69e-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: 127.28  E-value: 9.69e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067      2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYpHKEVLADAKIMDGGHFESQL---LFDAGA 78
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVARAaraAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     79 DYVTVLGVTDVLTIQSCIRAAKEAG-KQVVVDM-----------ICVDDLPARVRLLEE--AGADMLAVHTGTDQQAAGR 144
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVltspgaedlqeLGDESLEEQVLRLAKlaKEAGLDGVVCSATEPELIR 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16766067    145 KPIDDlitmlkvrrKARIAVAGGISSQ---TVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:smart00934 160 RALGP---------DFLILTPGIGDQGrvaTPAVAIGAGADIIVVGRPITQAADPVEAAEAI 212
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
3-203 7.86e-36

3-dehydro-L-gulonate-6-phosphate decarboxylase;


Pssm-ID: 237344  Cd Length: 216  Bit Score: 125.43  E-value: 7.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    3 LQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYVT 82
Cdd:PRK13306   6 LQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAGADWVT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   83 VLGVTDVLTIQSCIRAAKEAGKQVVVDMI---CVDDlparVRLLEEAGADMLAVHTGTDQQAAGRK-PIDDLITMLKVRR 158
Cdd:PRK13306  86 VICAAHIPTIKAALKVAKEFNGEIQIELYgnwTWEQ----AQQWRDAGISQVIYHRSRDAQLAGVAwGEKDLNKVKKLSD 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 16766067  159 KA-RIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:PRK13306 162 MGfKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAF 207
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 1-203 6.79e-33

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: 117.75  E-value: 6.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     1 MKLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKypHKEVLADAKIMDGGHFESQ---LLFDAG 77
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKqakYKAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    78 ADYVTVLGVTDVLTIQSCIRAAKEAG-KQVVVDMICVDDLPARVRLLEEaGADMLAVHTGTDQQA-----------AGRK 145
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDL-GYTQEIVHRAADLAAgvdgvvasateALRE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   146 PIDDLITMLK-VRrkARIAVAGGISSQTVKDYALL-GPDVVIVGSAITHAADPAGEARKI 203
Cdd:pfam00215 158 ILPDFLILTPgIG--LQGGDAGGQQRVTTPAVAKEaGADIIIVGRGITGAGDPVAAARAI 215
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
3-203 3.66e-28

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 108.95  E-value: 3.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    3 LQLALDELTLpEAMVFMDKVVDDVD--IIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADY 80
Cdd:PRK13307 175 LQVALDLPDL-EEVERVLSQLPKSDhiIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATADA 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   81 VTVLGVTDVLTIQSCIRAAKEAGKQVVVDMICVDDLPARVRLLEEAgADMLAVHTGTDQQAAgRKPIDDLITMLKVRRKA 160
Cdd:PRK13307 254 VVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLKVK-PDVVELHRGIDEEGT-EHAWGNIKEIKKAGGKI 331

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16766067  161 RIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:PRK13307 332 LVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAEDF 374
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
3-205 5.31e-23

3-keto-L-gulonate-6-phosphate decarboxylase UlaD;


Pssm-ID: 183962  Cd Length: 218  Bit Score: 92.18  E-value: 5.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    3 LQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPHKEVLADAKIMDGGHFESQLLFDAGADYVT 82
Cdd:PRK13305   6 LQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANWMT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   83 VLGVTDVLTIQSCIRAAKEAGKQVVVDMI---CVDDLPARVRLleeaGADMLAVHTGTDQQAAGRKPIDDLITMLKVRRK 159
Cdd:PRK13305  86 IICAAPLATVEKGHAVAQRCGGEIQIELFgnwTLDDARDWHRI----GVRQAIYHRGRDAQASGQQWGEADLARMKALSD 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 16766067  160 ARIA--VAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKISQ 205
Cdd:PRK13305 162 IGLElsITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHA 209
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 2-205 1.14e-15

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 72.32  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    2 KLQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKYPhkeVLADAKIMD---GGHFESQLLFDAGA 78
Cdd:PRK13813   5 RIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADipnTNRLICEAVFEAGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   79 DYVTVLGVTDVLTIQSCIRAAKEAGKQV--VVDMI----------CVDDLparVRLLEEAGAD-MLAVHTGTDQQAAGRK 145
Cdd:PRK13813  82 WGIIVHGFTGRDSLKAVVEAAAESGGKVfvVVEMShpgalefiqpHADKL---AKLAQEAGAFgVVAPATRPERVRYIRS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16766067  146 PIDDLITMlkvrrkariaVAGGISSQTVK--DYALLGPDVVIVGSAITHAADPAGEARKISQ 205
Cdd:PRK13813 159 RLGDELKI----------ISPGIGAQGGKaaDAIKAGADYVIVGRSIYNAADPREAAKAINE 210
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 5-203 3.41e-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: 60.27  E-value: 3.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   5 LALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKypHKEVLADAKIMDGGH-----FESqlLFDAGAD 79
Cdd:cd04725   3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL--GFLVFLDLKLGDIPNtvaaaAEA--LLGLGAD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  80 YVTVLGVTDVLTIQSCIRAAKEAGKQVVV-------------DMICVDDLP---ARVRLLEEAGADMLAVHtGTDQQAAG 143
Cdd:cd04725  79 AVTVHPYGGSDMLKAALEAAEEKGKGLFAvtvlsspgaldlqEGIPGSLEDlveRLAKLAREAGVDGVVCG-ATEPEALR 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16766067 144 RKPIDDLITM-----LKVRRKARIAVAggissqTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:cd04725 158 RALGPDFLILtpgigAQGSGDDQKRGG------TPEDAIRAGADYIVVGRPITQAADPVAAAEAI 216
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 3-203 1.97e-09

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: 55.44  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067     3 LQLALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKypHKEVLADAKIMDGGHFESQL---LFDAGAD 79
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKL--NKLIFLDLKFADIPNTVKLQyesKIKLGAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067    80 YVTVLGVTDVLTIQSCIRAAKEAGKQ---VVVDM-----ICVDDLPAR--VRLLEEAGA-DMLAVHTGTDQQAAGRKPID 148
Cdd:TIGR01740  79 MVNVHGFAGSESVEAAKEAASEFGRRgllAVTELtsmgsEEYGEDTMEkvVEYAKEAKEfGLIGPVCSAEEAKEIRKATG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16766067   149 DLITMLKVRRKARIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:TIGR01740 159 DFLILTPGIRLDSKDADDQKRVVTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRI 213
PyrF COG0284
Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5 ...
 5-203 4.15e-05

Orotidine-5'-phosphate decarboxylase [Nucleotide transport and metabolism]; Orotidine-5'-phosphate decarboxylase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440053  Cd Length: 228  Bit Score: 42.78  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067   5 LALDELTLPEAMVFMDKVVDDVDIIEVGTPFLIREGVNAIKAIKEKypHKEVLADAKIMDGGH-----FESqlLFDAGAD 79
Cdd:COG0284   7 VALDLPDAAEALAIVDALADLVCAYKPGLALFEAYGPEGVEALKER--GLPVFLDLKRHDIPNtvaaaARA--AAELGVD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  80 YVTV---LGVTdvlTIQSCIRAAKEAGKQVVV------------DMICVDDLPARV-----RLLEEAGADMLAVhtGTdQ 139
Cdd:COG0284  83 AVTVhayGGRD---MLEPALEAADESGKGVFAvtvltspgaadlQELGIEGPLYEVvlrlaKLAKEAGLDGVVC--SA-T 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16766067 140 QAAgrkpiddlitmlKVRRKA---RIAVAGGISSQ-----------TVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:COG0284 157 EAA------------ALRAALgpdFLLLTPGIRPQggdagdqkrvgTPAEAIAAGADYLVVGRPITYAGDPRAAAEAI 222
NadC COG0157
Nicotinate-nucleotide pyrophosphorylase [Coenzyme transport and metabolism]; ...
 156-197 1.19e-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: 41.93  E-value: 1.19e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 16766067 156 VRRKARIAVAGGISSQTVKDYALLGPDVVIVGsAITHAADPA 197
Cdd:COG0157 224 LRGRALLEASGGITLENIRAYAETGVDYISVG-ALTHSAPAL 264
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 158-203 2.35e-04

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: 40.83  E-value: 2.35e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16766067 158 RKARIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:COG0036 166 LDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAAL 211
QPRTase_NadC cd01568
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ...
 150-197 2.45e-04

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: 40.92  E-value: 2.45e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16766067 150 LITMLKVRRKARIAVAGGISSQTVKDYALLGPDVVIVGsAITHAADPA 197
Cdd:cd01568 218 AVKLLKGLPRVLLEASGGITLENIRAYAETGVDVISTG-ALTHSAPAL 264
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-188 4.66e-04

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: 39.88  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  26 VDIIEVGTPFLIREGVNAIK----AIKEKYPHKEVLADAKIMDGGHFES---QLLFDAGADYVTVLGVTDVLT--IQSCI 96
Cdd:cd04722  26 ADAIIVGTRSSDPEEAETDDkevlKEVAAETDLPLGVQLAINDAAAAVDiaaAAARAAGADGVEIHGAVGYLAreDLELI 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  97 RAAKEAGKQVVVDMICVDDLPARVRLLEEAGADMLAVHTGTDQQAAGRKPIDDLITMLKVRRKARIAV--AGGISS-QTV 173
Cdd:cd04722 106 RELREAVPDVKVVVKLSPTGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPViaGGGINDpEDA 185

                       170
                ....*....|....*
gi 16766067 174 KDYALLGPDVVIVGS 188
Cdd:cd04722 186 AEALALGADGVIVGS 200
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 142-203 6.73e-04

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: 39.39  E-value: 6.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16766067 142 AGRKPIDDliTMLKVRR----------KARIAVAGGISSQTVKDYALLGPDVVIVGSAITHAADPAGEARKI 203
Cdd:cd00429 141 GGQKFIPE--VLEKIRKlrelipennlNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKEL 210
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 117-205 1.58e-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: 37.88  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067 117 PARVRLLEEAGADMLAV----HTGTDQQAAGRKPIDDLitmLKVRRKARI-AVA-GGISSQTVKDYALLGPDVVIVGSAI 190
Cdd:cd00564 105 LEEALRAEELGADYVGFgpvfPTPTKPGAGPPLGLELL---REIAELVEIpVVAiGGITPENAAEVLAAGADGVAVISAI 181

                        90
                ....*....|....*
gi 16766067 191 THAADPAGEARKISQ 205
Cdd:cd00564 182 TGADDPAAAARELLA 196
modD_like cd01573
ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC ...
 43-194 4.47e-03

ModD; Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase) present in some modABC operons in bacteria, which are involved in molybdate transport. In general, QPRTases are part of the de novo synthesis pathway of NAD in both prokaryotes and eukaryotes. They catalyse the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide.


Pssm-ID: 238807 [Multi-domain]  Cd Length: 272  Bit Score: 37.28  E-value: 4.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  43 AIKAIKE--KYPHKevladakimdGGHFESQLLFdagADYVTVLGVTDVLTIQSCIRAAkEAGKQVVVDmicVDDLpARV 120
Cdd:cd01573 135 ALKAILAggAVPHR----------LGLSETILVF---AEHRAFLGGPEPLKALARLRAT-APEKKIVVE---VDSL-EEA 196

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16766067 121 RLLEEAGADMLAVHTGTDQQAAgrkpidDLITMLKVRRK-ARIAVAGGISSQTVKDYALLGPDvVIVGSAITHAA 194
Cdd:cd01573 197 LAAAEAGADILQLDKFSPEELA------ELVPKLRSLAPpVLLAAAGGINIENAAAYAAAGAD-ILVTSAPYYAK 264
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 39-192 5.93e-03

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 36.40  E-value: 5.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  39 EGVNAIKA---------IKEKYPHKEVLADAKIMdgghfESQLLFDAGADYVTvLGVT-----DVLTIQSCIRAAKEAGK 104
Cdd:cd04729  50 EDIRAIRArvdlpiiglIKRDYPDSEVYITPTIE-----EVDALAAAGADIIA-LDATdrprpDGETLAELIKRIHEEYN 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067 105 QVVV-DMICVDDlparVRLLEEAGADML--AVHTGTDQQAAGRKPIDDLITMLKVRRKARIAVAGGISS-QTVKDYALLG 180
Cdd:cd04729 124 CLLMaDISTLEE----ALNAAKLGFDIIgtTLSGYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSpEQAAKALELG 199

                       170
                ....*....|..
gi 16766067 181 PDVVIVGSAITH 192
Cdd:cd04729 200 ADAVVVGSAITR 211
thiE PRK00043
thiamine phosphate synthase;
117-207 9.02e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 35.93  E-value: 9.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16766067  117 PARVRLLEEAGADMLAV----HTGTDQqaaGRKPIDDLITMLKVRRKAR---IAVAGGISSQTVKDYALLGPDVVIVGSA 189
Cdd:PRK00043 114 LEEAAAALAAGADYVGVgpifPTPTKK---DAKAPQGLEGLREIRAAVGdipIVAIGGITPENAPEVLEAGADGVAVVSA 190

                         90
                 ....*....|....*...
gi 16766067  190 ITHAADPAGEARKISQVL 207
Cdd:PRK00043 191 ITGAEDPEAAARALLAAF 208
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
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