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Conserved domains on  [gi|1714026156|gb|QDW85360|]
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3-hexulose-6-phosphate synthase [Staphylococcus pasteuri]

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 1.04e-94

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: 274.63  E-value: 1.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   2 ELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIKNSK 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1714026156 162 VAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAI 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 1.04e-94

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: 274.63  E-value: 1.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   2 ELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIKNSK 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1714026156 162 VAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAI 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-209 2.11e-83

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 246.23  E-value: 2.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADV 80
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIkNS 160
Cdd:COG0269    84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKELV-GV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1714026156 161 KVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAIEG 209
Cdd:COG0269   163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 1-203 8.81e-73

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: 218.99  E-value: 8.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADV 80
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKeLDEMGADYIAVHTGYDLQAEG-QSPLDSLRKVKSVIkN 159
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKLL-G 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1714026156 160 SKVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQC 203
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 3-208 1.15e-57

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 187.53  E-value: 1.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKK-VEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVV 81
Cdd:PRK07028    6 LQVALDLLELDRAVEIAKEaVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIkNSK 161
Cdd:PRK07028   86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELLKEVSEEV-SIP 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1714026156 162 VAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAIE 208
Cdd:PRK07028  165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAID 211
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 1-202 1.79e-38

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: 132.00  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNEniNNAKVLADLKIMDAADYEVSQA---VKFG 77
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRK--HGFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  78 ADVVTILGVAEDASIKAAVEEAHKNDKQLL-VDMIAVQDLEKRAKELDeMGADYIAVHTGYDLQAE-------GQSPLDS 149
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGRGLLlVAELSSKGSLDLQEEGD-LGYTQEIVHRAADLAAGvdgvvasATEALRE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1714026156 150 LRKVKSVIK---NSKVAVAGGIKPDTIKDIVAED-PDLVIVGGGIANADDPVEAAKQ 202
Cdd:pfam00215 158 ILPDFLILTpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARA 214
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 3-202 1.82e-33

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: 118.81  E-value: 1.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156    3 LQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLnENINNAKVLADLKIMDAADYE---VSQAVKFGAD 79
Cdd:smart00934   2 LIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL-KELFGFPVFLDLKLHDIPNTVaraARAAAELGAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   80 VVTILGVAEDASIKAAVEEAHKND-KQLLVDMIAVQDLEKRAKELDE-------------MGADYIAVHTGYDLQAegqs 145
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDEsleeqvlrlaklaKEAGLDGVVCSATEPE---- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  146 pldslRKVKSVIKNSKVAVAG-GIKPDTIKDIVA--EDPDLVIVGGGIANADDPVEAAKQ 202
Cdd:smart00934 157 -----LIRRALGPDFLILTPGiGDQGRVATPAVAigAGADIIVVGRPITQAADPVEAAEA 211
 
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 1.04e-94

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: 274.63  E-value: 1.04e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   2 ELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVV 81
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIKNSK 161
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQNPFEDLQTILKLVKEAR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1714026156 162 VAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAI 207
Cdd:TIGR03128 161 VAVAGGINLDTIPDVIKLGPDIVIVGGAITKAADPAEAARQIRKLI 206
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-209 2.11e-83

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 246.23  E-value: 2.11e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADV 80
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGADI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIkNS 160
Cdd:COG0269    84 VTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGGSPLDDLKKIKELV-GV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1714026156 161 KVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAIEG 209
Cdd:COG0269   163 PVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDK 211
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 1-203 8.81e-73

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: 218.99  E-value: 8.81e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADV 80
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKeLDEMGADYIAVHTGYDLQAEG-QSPLDSLRKVKSVIkN 159
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAK-LLKLGVDIVILHRGIDAQAAGgWWPEDDLKKVKKLL-G 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1714026156 160 SKVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQC 203
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 3-208 1.15e-57

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 187.53  E-value: 1.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKK-VEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVV 81
Cdd:PRK07028    6 LQVALDLLELDRAVEIAKEaVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGADIV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMGADYIAVHTGYDLQAEGQSPLDSLRKVKSVIkNSK 161
Cdd:PRK07028   86 CILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQMLGKDPLELLKEVSEEV-SIP 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1714026156 162 VAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAIE 208
Cdd:PRK07028  165 IAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAID 211
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 1-202 1.79e-38

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: 132.00  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   1 MELQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNEniNNAKVLADLKIMDAADYEVSQA---VKFG 77
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRK--HGFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  78 ADVVTILGVAEDASIKAAVEEAHKNDKQLL-VDMIAVQDLEKRAKELDeMGADYIAVHTGYDLQAE-------GQSPLDS 149
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGRGLLlVAELSSKGSLDLQEEGD-LGYTQEIVHRAADLAAGvdgvvasATEALRE 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1714026156 150 LRKVKSVIK---NSKVAVAGGIKPDTIKDIVAED-PDLVIVGGGIANADDPVEAAKQ 202
Cdd:pfam00215 158 ILPDFLILTpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARA 214
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 3-202 1.82e-33

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: 118.81  E-value: 1.82e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156    3 LQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLnENINNAKVLADLKIMDAADYE---VSQAVKFGAD 79
Cdd:smart00934   2 LIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKEL-KELFGFPVFLDLKLHDIPNTVaraARAAAELGAD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   80 VVTILGVAEDASIKAAVEEAHKND-KQLLVDMIAVQDLEKRAKELDE-------------MGADYIAVHTGYDLQAegqs 145
Cdd:smart00934  81 AVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDEsleeqvlrlaklaKEAGLDGVVCSATEPE---- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  146 pldslRKVKSVIKNSKVAVAG-GIKPDTIKDIVA--EDPDLVIVGGGIANADDPVEAAKQ 202
Cdd:smart00934 157 -----LIRRALGPDFLILTPGiGDQGRVATPAVAigAGADIIVVGRPITQAADPVEAAEA 211
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
3-202 1.32e-29

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 112.80  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKKVEEYvD--IVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADV 80
Cdd:PRK13307  175 LQVALDLPDLEEVERVLSQLPKS-DhiIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATADA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKELDEMgADYIAVHTGYDLQaEGQSPLDSLRKVKSVIKNS 160
Cdd:PRK13307  254 VVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLKVK-PDVVELHRGIDEE-GTEHAWGNIKEIKKAGGKI 331

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1714026156 161 KVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQ 202
Cdd:PRK13307  332 LVAVAGGVRVENVEEALKAGADILVVGRAITKSKDVRRAAED 373
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
3-207 7.00e-26

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 99.23  E-value: 7.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVVT 82
Cdd:PRK13306    6 LQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAGADWVT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  83 ILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEkRAKELDEMGADYIAVHTGYDLQAEGQS-PLDSLRKVKSVIKNS- 160
Cdd:PRK13306   86 VICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWE-QAQQWRDAGISQVIYHRSRDAQLAGVAwGEKDLNKVKKLSDMGf 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1714026156 161 KVAVAGGIKPDTI---KDIVAEdpdLVIVGGGIANADDPVEAAKQCRDAI 207
Cdd:PRK13306  165 KVSVTGGLVVEDLklfKGIPVK---TFIAGRAIRGAADPAAAARAFKDEI 211
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
3-208 6.77e-20

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 83.71  E-value: 6.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENINNAKVLADLKIMDAADYEVSQAVKFGADVVT 82
Cdd:PRK13305    6 LQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANWMT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  83 ILGVAEDASIKAAVEEAHKNDKQLLVDMIAVQDLEKrAKELDEMGADYIAVHTGYDLQAEGQSPLDS-LRKVKSVIK-NS 160
Cdd:PRK13305   86 IICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDD-ARDWHRIGVRQAIYHRGRDAQASGQQWGEAdLARMKALSDiGL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1714026156 161 KVAVAGGIKPDTI---KDIvaeDPDLVIVGGGIANADDPVEAAKQCRDAIE 208
Cdd:PRK13305  165 ELSITGGITPADLplfKDI---RVKAFIAGRALAGAANPAQVAADFHAQID 212
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 5-210 5.48e-16

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 73.09  E-value: 5.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   5 LAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLnenINNAKVLADLKIMDAADYE---VSQAVKFGADVV 81
Cdd:PRK13813    8 LALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEEL---KRYAPVIADLKVADIPNTNrliCEAVFEAGAWGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  82 TILGVAEDASIKAAVEEAHKNDKQ--LLVDMI---AVQDLEKRAKELDEMgadyiAVHTG-YDLQAEGQSPlDSLRKVKS 155
Cdd:PRK13813   85 IVHGFTGRDSLKAVVEAAAESGGKvfVVVEMShpgALEFIQPHADKLAKL-----AQEAGaFGVVAPATRP-ERVRYIRS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1714026156 156 VIKNSKVAVAGGIKPD--TIKDIVAEDPDLVIVGGGIANADDPVEAAKQCRDAIEGK 210
Cdd:PRK13813  159 RLGDELKIISPGIGAQggKAADAIKAGADYVIVGRSIYNAADPREAAKAINEEIRGA 215
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 5-202 6.64e-14

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: 67.59  E-value: 6.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   5 LAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENinNAKVLADLKIMD----AADYeVSQAVKFGADV 80
Cdd:cd04725     3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL--GFLVFLDLKLGDipntVAAA-AEALLGLGADA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  81 VTILGVAEDASIKAAVEEAHKNDKQLLV---------------DMIAVQDL-EKRAKELDEMGADYIAVhtgydlqaegq 144
Cdd:cd04725    80 VTVHPYGGSDMLKAALEAAEEKGKGLFAvtvlsspgaldlqegIPGSLEDLvERLAKLAREAGVDGVVC----------- 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1714026156 145 SPLDSLRKVKSVIKNSKVaVAGGIKPD----------TIKDIVAEDPDLVIVGGGIANADDPVEAAKQ 202
Cdd:cd04725   149 GATEPEALRRALGPDFLI-LTPGIGAQgsgddqkrggTPEDAIRAGADYIVVGRPITQAADPVAAAEA 215
pyrF TIGR01740
orotidine 5'-phosphate decarboxylase, subfamily 1; This model represents orotidine 5 ...
 3-204 2.71e-12

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: 63.14  E-value: 2.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156   3 LQLAIDLLNKEEAAELAKKVEEYVDIVEIGTPIVINEGLPAVQHLNENinNAKVLADLKIMDAaDYEVSQAVKF----GA 78
Cdd:TIGR01740   1 LIVALDVTTKEEALDLADSLGEEICVIKVGYDLLLSGGEKIIDELAKL--NKLIFLDLKFADI-PNTVKLQYESkiklGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  79 DVVTILGVAEDASIKAAVEEAHKNDKQLL-------------VDMIAVQDLEKRAKELDEMGADyiavhtGYDLQAEgqs 145
Cdd:TIGR01740  78 DMVNVHGFAGSESVEAAKEAASEFGRRGLlavteltsmgseeYGEDTMEKVVEYAKEAKEFGLI------GPVCSAE--- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 146 pldsLRKVKSVIKNSKVAVAGGIKPD-----------TIKDIVAEDPDLVIVGGGIANADDPVEAAKQCR 204
Cdd:TIGR01740 149 ----EAKEIRKATGDFLILTPGIRLDskdaddqkrvvTLEEAKEAGADVIIVGRGIYAAEDPVEAAKRIR 214
thiE PRK00043
thiamine phosphate synthase;
117-208 7.31e-07

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 47.87  E-value: 7.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 117 EKRAKELDEMGADYIAV----HTGYDLQAEGQSPLDSLRKVKSVIKNSKVAVAGGIKPDTIKDIVAEDPDLVIVGGGIAN 192
Cdd:PRK00043  114 LEEAAAALAAGADYVGVgpifPTPTKKDAKAPQGLEGLREIRAAVGDIPIVAIGGITPENAPEVLEAGADGVAVVSAITG 193

                          90
                  ....*....|....*.
gi 1714026156 193 ADDPVEAAKQCRDAIE 208
Cdd:PRK00043  194 AEDPEAAARALLAAFR 209
PRK07695 PRK07695
thiazole tautomerase TenI;
113-209 1.15e-05

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 44.24  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 113 VQDLEKrAKELDEMGADYIAVHTGYD------LQAEGqspLDSLRKVKSVIKNSKVAVaGGIKPDTIKDIVAEDPDLVIV 186
Cdd:PRK07695  102 VHSLEE-AIQAEKNGADYVVYGHVFPtdckkgVPARG---LEELSDIARALSIPVIAI-GGITPENTRDVLAAGVSGIAV 176

                          90       100
                  ....*....|....*....|...
gi 1714026156 187 GGGIANADDPVEAAKQCRDAIEG 209
Cdd:PRK07695  177 MSGIFSSANPYSKAKRYAESIKK 199
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 120-209 1.62e-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: 44.02  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 120 AKELDEMGADYIAV--------HTGYDLQAEgqspLDSLRKVKSVIkNSKVAVAGGIKPDTIKDIVAEDPDLVIVGGGIA 191
Cdd:COG0352   113 ALRAEEAGADYVGFgpvfptptKPGAPPPLG----LEGLAWWAELV-EIPVVAIGGITPENAAEVLAAGADGVAVISAIW 187

                          90
                  ....*....|....*...
gi 1714026156 192 NADDPVEAAKQCRDAIEG 209
Cdd:COG0352   188 GAPDPAAAARELRAALEA 205
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 120-205 4.07e-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: 42.51  E-value: 4.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 120 AKELDEMGADYIAV----HTgyDLQAEGQSP--LDSLRKVKSVIKNSKVAVaGGIKPDTIKDIVAEDPDLVIVGGGIANA 193
Cdd:cd00564   108 ALRAEELGADYVGFgpvfPT--PTKPGAGPPlgLELLREIAELVEIPVVAI-GGITPENAAEVLAAGADGVAVISAITGA 184

                          90
                  ....*....|..
gi 1714026156 194 DDPVEAAKQCRD 205
Cdd:cd00564   185 DDPAAAARELLA 196
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 147-204 5.84e-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: 5.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1714026156 147 LDSLRKVKSVIKNS----KVAVAGGIKPDTIKDIVAEDPDLVIVGGGIANADDPVEAAKQCR 204
Cdd:cd00429   150 LEKIRKLRELIPENnlnlLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
PRK13802 PRK13802
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
 67-202 8.38e-04

bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 184335 [Multi-domain]  Cd Length: 695  Bit Score: 39.63  E-value: 8.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156  67 DYEVSQAVKFGADVVTILGVA-EDASIKAAVEEAHKNDKQLLVDMIAVQDLEKRAKEldemGADYIAVHTG--YDLQAE- 142
Cdd:PRK13802  123 DYQIWEARAHGADLVLLIVAAlDDAQLKHLLDLAHELGMTVLVETHTREEIERAIAA----GAKVIGINARnlKDLKVDv 198

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1714026156 143 GQSPLDSLRKVKSVIKNSKVAVAGGIKpdtIKDIVAEDPDLVIVGGGIANADDPVEAAKQ 202
Cdd:PRK13802  199 NKYNELAADLPDDVIKVAESGVFGAVE---VEDYARAGADAVLVGEGVATADDHELAVER 255
 
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.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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