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Conserved domains on  [gi|836588565|ref|WP_047745809|]
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MULTISPECIES: 3-keto-L-gulonate-6-phosphate decarboxylase UlaD [Enterobacter cloacae complex]

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 1.49e-141

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


:

Pssm-ID: 183962  Cd Length: 218  Bit Score: 394.18  E-value: 1.49e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565 161 DIGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIRDIWGA 217
Cdd:PRK13305 161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWGG 217
 
Name Accession Description Interval E-value
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-217 1.49e-141

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 394.18  E-value: 1.49e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565 161 DIGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIRDIWGA 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 2.31e-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: 2.31e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   4 PLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAGANW 83
Cdd:cd04726    1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  84 MTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALsdIG 163
Cdd:cd04726   81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 836588565 164 LQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAF 207
Cdd:cd04726  159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-212 3.15e-84

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 248.54  E-value: 3.15e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:COG0269    1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHW-TLDDARAWHHIGVKQAIYHRGRDAQASGQQwDEADLAKMKAL 159
Cdd:COG0269   81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 836588565 160 SdiGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIR 212
Cdd:COG0269  160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAID 210
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-207 1.38e-45

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: 150.49  E-value: 1.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565    4 PLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQcpDKIIVADWKVADAGETLAEQA---FGAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   81 ANWMTIICAAPLATVERGHEVALRRG-GEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQA-------SGQQWDEAD 152
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvdgvvaSATEALREI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565  153 LAKMKALS-DIGLQLSITGGITPADLPLFKQIN-VKAFIAGRALAGAANPPQVAQAF 207
Cdd:pfam00215 159 LPDFLILTpGIGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-207 2.07e-40

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: 137.30  E-value: 2.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565     5 LLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCpDKIIVADWKVADAGET---LAEQAFGAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTvarAARAAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565    82 NWMTIICAAPLATVERGHEVALRRG-GEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQ-----QWDEADLAK 155
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLdgvvcSATEPELIR 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 836588565   156 MKALSDigLQLSITG-GITPADLPLFKQINVKA--FIAGRALAGAANPPQVAQAF 207
Cdd:smart00934 160 RALGPD--FLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQAADPVEAAEAI 212
 
Name Accession Description Interval E-value
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-217 1.49e-141

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 394.18  E-value: 1.49e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:PRK13305   1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALS 160
Cdd:PRK13305  81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565 161 DIGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIRDIWGA 217
Cdd:PRK13305 161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWGG 217
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-216 2.77e-107

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 307.24  E-value: 2.77e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:PRK13306   1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALS 160
Cdd:PRK13306  81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 836588565 161 DIGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIRDIWG 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 2.31e-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: 2.31e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   4 PLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAGANW 83
Cdd:cd04726    1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  84 MTIICAAPLATVERGHEVALRRGGEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQQWDEADLAKMKALsdIG 163
Cdd:cd04726   81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 836588565 164 LQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAF 207
Cdd:cd04726  159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-212 3.15e-84

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 248.54  E-value: 3.15e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAG 80
Cdd:COG0269    1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  81 ANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHW-TLDDARAWHHIGVKQAIYHRGRDAQASGQQwDEADLAKMKAL 159
Cdd:COG0269   81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 836588565 160 SdiGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVAQAFHSHIR 212
Cdd:COG0269  160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAID 210
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-207 1.38e-45

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: 150.49  E-value: 1.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565    4 PLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQcpDKIIVADWKVADAGETLAEQA---FGAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   81 ANWMTIICAAPLATVERGHEVALRRG-GEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQA-------SGQQWDEAD 152
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvdgvvaSATEALREI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565  153 LAKMKALS-DIGLQLSITGGITPADLPLFKQIN-VKAFIAGRALAGAANPPQVAQAF 207
Cdd:pfam00215 159 LPDFLILTpGIGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-207 2.07e-40

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: 137.30  E-value: 2.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565     5 LLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCpDKIIVADWKVADAGET---LAEQAFGAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTvarAARAAAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565    82 NWMTIICAAPLATVERGHEVALRRG-GEIQMELFGHWTLDDARAWHHIGVKQAIYHRGRDAQASGQ-----QWDEADLAK 155
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLdgvvcSATEPELIR 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 836588565   156 MKALSDigLQLSITG-GITPADLPLFKQINVKA--FIAGRALAGAANPPQVAQAF 207
Cdd:smart00934 160 RALGPD--FLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQAADPVEAAEAI 212
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 1-204 2.14e-19

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 85.46  E-value: 2.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQrDVA--TLADHVDIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFG 78
Cdd:PRK07028   1 MERPILQVALDLLELDRAV-EIAkeAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  79 AGANWMTIICAAPLATVERGHEVALRRGGEIQMELFGHWT-LDDARAWHHIGVKQAIYHRGRDAQASGQqwDEADLAKmK 157
Cdd:PRK07028  80 AGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDpVKRAVELEELGVDYINVHVGIDQQMLGK--DPLELLK-E 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 836588565 158 ALSDIGLQLSITGGITPADLPLFKQINVKAFIAGRALAGAANPPQVA 204
Cdd:PRK07028 157 VSEEVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAA 203
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
4-213 2.01e-18

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 82.37  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   4 PLLQLALDHTSLQAAQRDVATL--ADHVdIVEAGTILCLTEGLNAVRALREQCPDKIIVADWKVADAGETLAEQAFGAGA 81
Cdd:PRK13307 173 PYLQVALDLPDLEEVERVLSQLpkSDHI-IIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADATA 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  82 NWMTIICAAPLATVERGHEVALRRGGEIQMELFGhwTLDDARAWHHIGVKQAI--YHRGRDAQASGQQWdeADLAKMKAL 159
Cdd:PRK13307 252 DAVVISGLAPISTIEKAIHEAQKTGIYSILDMLN--VEDPVKLLESLKVKPDVveLHRGIDEEGTEHAW--GNIKEIKKA 327

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 836588565 160 SDIGLqLSITGGITPADLPlfKQINVKA--FIAGRALAGAANPPQVAQAFHSHIRD 213
Cdd:PRK13307 328 GGKIL-VAVAGGVRVENVE--EALKAGAdiLVVGRAITKSKDVRRAAEDFLNKLKP 380
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 8-207 1.24e-07

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: 50.25  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   8 LALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCpdKIIVADWKVADAGETLAEQAFGAGANWMTII 87
Cdd:cd04725    3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELRELG--FLVFLDLKLGDIPNTVAAAAEALLGLGADAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565  88 CAAPLAtverGHEV---ALRRGGEIQMELFG-----HWTLDDARAWHHIGVKQAIYHRGRDAQASGQ-----QWDEADLA 154
Cdd:cd04725   81 TVHPYG----GSDMlkaALEAAEEKGKGLFAvtvlsSPGALDLQEGIPGSLEDLVERLAKLAREAGVdgvvcGATEPEAL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 836588565 155 KMKALSD-------IGLQLSITG---GITPADLplfkqinVKAF----IAGRALAGAANPPQVAQAF 207
Cdd:cd04725  157 RRALGPDfliltpgIGAQGSGDDqkrGGTPEDA-------IRAGadyiVVGRPITQAADPVAAAEAI 216
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-86 1.72e-05

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 44.20  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836588565   1 MSRPLLQLALDHTSLQAAQRDVATLADHVDIVEAGTILCLTEGLNAVRALREQCPdkiIVADWKVADAGET---LAEQAF 77
Cdd:PRK13813   1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPNTnrlICEAVF 77


                 ....*....
gi 836588565  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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