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Conserved domains on  [gi|16131452|ref|NP_418038|]
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3-keto-L-gulonate-6-phosphate decarboxylase SgbH [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

3-dehydro-L-gulonate-6-phosphate decarboxylase( domain architecture ID 10793779)

3-dehydro-L-gulonate-6-phosphate decarboxylase catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-217 1.40e-145

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


:

Pssm-ID: 183962  Cd Length: 218  Bit Score: 404.20  E-value: 1.40e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131452  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWGG 217
Cdd:PRK13305 161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWGG 217
 
Name Accession Description Interval E-value
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-217 1.40e-145

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 404.20  E-value: 1.40e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131452  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWGG 217
Cdd:PRK13305 161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWGG 217
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 4-207 2.59e-86

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: 253.66  E-value: 2.59e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   4 PLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANW 83
Cdd:cd04726   1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  84 MTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALsdIG 163
Cdd:cd04726  81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16131452 164 LELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDF 207
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-214 1.19e-83

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 247.38  E-value: 1.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:COG0269   1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNW-TLDDARDWHRIGVRQAIYHRGRDAQASGQQwGEADLARMKAL 159
Cdd:COG0269  81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131452 160 SdiGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAI 214
Cdd:COG0269 160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-204 6.03e-46

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: 151.65  E-value: 6.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452     4 PLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQcpDKIIVADWKVADAGETLAQQA---FGAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    81 ANWMTIICAAPLATVEKGHAMAQRCG-GEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQA--SGQQWGEADLARMK 157
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALREI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16131452   158 AL------SDIGLELSITGGITPADLPLFKDIR-VKAFIAGRALAGAANPAQVA 204
Cdd:pfam00215 159 LPdfliltPGIGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAA 212
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-204 3.11e-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: 129.21  E-value: 3.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452      5 LLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCpDKIIVADWKVADAGET---LAQQAFGAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTvarAARAAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452     82 NWMTIICAAPLATVEKGHAMAQRCG-GEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGqQWG------EADLA 154
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAG-LDGvvcsatEPELI 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16131452    155 RMKALSDigLELSITG-GITPADLPLFKDIRVKA--FIAGRALAGAANPAQVA 204
Cdd:smart00934 159 RRALGPD--FLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQAADPVEAA 209
 
Name Accession Description Interval E-value
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-217 1.40e-145

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 404.20  E-value: 1.40e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 16131452  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWGG 217
Cdd:PRK13305 161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWGG 217
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-216 1.01e-106

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 306.08  E-value: 1.01e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:PRK13306   1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160
Cdd:PRK13306  81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16131452  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIWG 216
Cdd:PRK13306 161 DMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAFKDEIAKYWG 216
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 4-207 2.59e-86

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: 253.66  E-value: 2.59e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   4 PLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGANW 83
Cdd:cd04726   1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  84 MTIICAAPLATVEKGHAMAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALsdIG 163
Cdd:cd04726  81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16131452 164 LELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDF 207
Cdd:cd04726 159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-214 1.19e-83

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 247.38  E-value: 1.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80
Cdd:COG0269   1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  81 ANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGNW-TLDDARDWHRIGVRQAIYHRGRDAQASGQQwGEADLARMKAL 159
Cdd:COG0269  81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16131452 160 SdiGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAI 214
Cdd:COG0269 160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-204 6.03e-46

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: 151.65  E-value: 6.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452     4 PLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQcpDKIIVADWKVADAGETLAQQA---FGAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    81 ANWMTIICAAPLATVEKGHAMAQRCG-GEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQA--SGQQWGEADLARMK 157
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALREI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16131452   158 AL------SDIGLELSITGGITPADLPLFKDIR-VKAFIAGRALAGAANPAQVA 204
Cdd:pfam00215 159 LPdfliltPGIGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAA 212
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-204 3.11e-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: 129.21  E-value: 3.11e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452      5 LLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCpDKIIVADWKVADAGET---LAQQAFGAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTvarAARAAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452     82 NWMTIICAAPLATVEKGHAMAQRCG-GEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGqQWG------EADLA 154
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAG-LDGvvcsatEPELI 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 16131452    155 RMKALSDigLELSITG-GITPADLPLFKDIRVKA--FIAGRALAGAANPAQVA 204
Cdd:smart00934 159 RRALGPD--FLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQAADPVEAA 209
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
4-207 1.71e-18

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 82.75  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    4 PLLQLALDHSSLEAAQRDVTLLKDSvD--IVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGA 81
Cdd:PRK13307 173 PYLQVALDLPDLEEVERVLSQLPKS-DhiIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   82 NWMTIICAAPLATVEKGHAMAQRCGGEIQIELFGnwTLDDARDWHRIGVRQAI--YHRGRDAQASGQQWGeaDLARMKAL 159
Cdd:PRK13307 252 DAVVISGLAPISTIEKAIHEAQKTGIYSILDMLN--VEDPVKLLESLKVKPDVveLHRGIDEEGTEHAWG--NIKEIKKA 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 16131452  160 SDIGLeLSITGGITPADLPlfKDIRVKA--FIAGRALAGAANPAQVAGDF 207
Cdd:PRK13307 328 GGKIL-VAVAGGVRVENVE--EALKAGAdiLVVGRAITKSKDVRRAAEDF 374
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 1-215 6.98e-16

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 75.44  E-value: 6.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEaaqRDVTLLKDSV----DIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQA 76
Cdd:PRK07028   1 MERPILQVALDLLELD---RAVEIAKEAVaggaDWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   77 FGAGANWMTIICAAPLATVEKGHAMAQRCGGEIQIELFG-NWTLDDARDWHRIGVRQAIYHRGRDAQASGQQwgEADLAR 155
Cdd:PRK07028  78 AKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINvPDPVKRAVELEELGVDYINVHVGIDQQMLGKD--PLELLK 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  156 mKALSDIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAGDFHAQIDAIW 215
Cdd:PRK07028 156 -EVSEEVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAIDSGK 214
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 8-204 4.07e-06

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: 46.02  E-value: 4.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452   8 LALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCpdKIIVADWKVADAGETLAQQAFGAGANWMTII 87
Cdd:cd04725   3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG--FLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452  88 CAAPLAtvekGHAMAQRC---GGEIQIELFG-----NWTLDDARDWHRIGVRQAIYHRGRDAQASGqQWG------EADL 153
Cdd:cd04725  81 TVHPYG----GSDMLKAAleaAEEKGKGLFAvtvlsSPGALDLQEGIPGSLEDLVERLAKLAREAG-VDGvvcgatEPEA 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131452 154 ARMKALSD-------IGLELSITG---GITPADLplfkdIRVKA--FIAGRALAGAANPAQVA 204
Cdd:cd04725 156 LRRALGPDfliltpgIGAQGSGDDqkrGGTPEDA-----IRAGAdyIVVGRPITQAADPVAAA 213
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-86 2.59e-05

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 43.43  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131452    1 MSRPLLQLALDHSSLEAAQRDVTLLKDSVDIVEAGTILCLNEGLGAVKALREQCPdkiIVADWKVADAGET---LAQQAF 77
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPNTnrlICEAVF 77


                 ....*....
gi 16131452   78 GAGAnWMTI 86
Cdd:PRK13813  78 EAGA-WGII 85
 
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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