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Conserved domains on  [gi|1476721357|gb|RIE80807|]
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3-keto-L-gulonate-6-phosphate decarboxylase UlaD [Shigella dysenteriae]

Protein Classification

3-keto-L-gulonate-6-phosphate decarboxylase UlaD( domain architecture ID 10014187)

3-keto-L-gulonate-6-phosphate decarboxylase UlaD catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P, and is involved in anaerobic L-ascorbate utilization

EC:  4.1.1.85
Gene Ontology:  GO:0000287|GO:0016831

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-216 6.95e-136

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


:

Pssm-ID: 237344  Cd Length: 216  Bit Score: 379.66  E-value: 6.95e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1476721357 161 DMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG 216
Cdd:PRK13306  161 DMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPAAAARAFKDEIAKYWG 216
 
Name Accession Description Interval E-value
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-216 6.95e-136

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 379.66  E-value: 6.95e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1476721357 161 DMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG 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 4.80e-91

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: 265.60  E-value: 4.80e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   4 PMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEANADW 83
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  84 VTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLsdMG 163
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1476721357 164 FKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQF 207
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-214 1.32e-89

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 262.41  E-value: 1.32e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:COG0269     1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYW-TWEQAQQWRDAGIQQVVYHRSRDAQAAGVAwGEADITAIKRL 159
Cdd:COG0269    81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476721357 160 SdmGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAEL 214
Cdd:COG0269   160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-207 2.35e-49

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: 160.12  E-value: 2.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   4 PMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALypHKIVLADAKIADAGKILSRMC---FEAN 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFN-GDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQA--AGVAWGEADIT--A 155
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALreI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1476721357 156 IKRLSDM----GFKVTVTGGLALEDLPLFKGIP-IHVFIAGRSIRDAASPVEAARQF 207
Cdd:pfam00215 159 LPDFLILtpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-207 1.73e-46

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: 152.71  E-value: 1.73e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357    5 MLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLaDAKIADAGKILSRMC---FEANA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELFGFPVFL-DLKLHDIPNTVARAAraaAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   82 DWVTVICCADINTAKGALDVAKEFN-GDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADIT---AIK 157
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLDGVVCSATepeLIR 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1476721357  158 RLSDMGFKVTVTGGLA-LEDLPLFKGIPIH--VFIAGRSIRDAASPVEAARQF 207
Cdd:smart00934 160 RALGPDFLILTPGIGDqGRVATPAVAIGAGadIIVVGRPITQAADPVEAAEAI 212
 
Name Accession Description Interval E-value
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-216 6.95e-136

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 379.66  E-value: 6.95e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1476721357 161 DMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG 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 4.80e-91

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: 265.60  E-value: 4.80e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   4 PMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEANADW 83
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  84 VTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLsdMG 163
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1476721357 164 FKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQF 207
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-214 1.32e-89

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 262.41  E-value: 1.32e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:COG0269     1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYW-TWEQAQQWRDAGIQQVVYHRSRDAQAAGVAwGEADITAIKRL 159
Cdd:COG0269    81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAGGS-PLDDLKKIKEL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1476721357 160 SdmGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAEL 214
Cdd:COG0269   160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDPAAAAREIREAIDKA 212
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-216 2.21e-88

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 259.36  E-value: 2.21e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEAN 80
Cdd:PRK13305    1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADITAIKRLS 160
Cdd:PRK13305   81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1476721357 161 DMGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSIAELWG 216
Cdd:PRK13305  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAANPAQVAADFHAQIDAIWG 216
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-207 2.35e-49

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: 160.12  E-value: 2.35e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   4 PMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALypHKIVLADAKIADAGKILSRMC---FEAN 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFN-GDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQA--AGVAWGEADIT--A 155
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGrGLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADLAAgvDGVVASATEALreI 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1476721357 156 IKRLSDM----GFKVTVTGGLALEDLPLFKGIP-IHVFIAGRSIRDAASPVEAARQF 207
Cdd:pfam00215 159 LPDFLILtpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAAARAI 215
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-207 1.73e-46

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: 152.71  E-value: 1.73e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357    5 MLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPHKIVLaDAKIADAGKILSRMC---FEANA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELFGFPVFL-DLKLHDIPNTVARAAraaAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   82 DWVTVICCADINTAKGALDVAKEFN-GDVQIELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVAWGEADIT---AIK 157
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGpGLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLDGVVCSATepeLIR 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1476721357  158 RLSDMGFKVTVTGGLA-LEDLPLFKGIPIH--VFIAGRSIRDAASPVEAARQF 207
Cdd:smart00934 160 RALGPDFLILTPGIGDqGRVATPAVAIGAGadIIVVGRPITQAADPVEAAEAI 212
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 1-211 1.10e-19

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 86.23  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYEttrlIAEE-----VDIIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRM 75
Cdd:PRK07028    1 MERPILQVALDLLELDRAVE----IAKEavaggADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  76 CFEANADWVTVICCADINTAKGALDVAKEFNGDVQIELTG-YWTWEQAQQWRDAGIQQVVYHRSRDAQAAGVawgeADIT 154
Cdd:PRK07028   77 AAKAGADIVCILGLADDSTIEDAVRAARKYGVRLMADLINvPDPVKRAVELEELGVDYINVHVGIDQQMLGK----DPLE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721357 155 AIKRLSD-MGFKVTVTGGLALEDLPLFKGIPIHVFIAGRSIRDAASPVEAARQFKRSI 211
Cdd:PRK07028  153 LLKEVSEeVSIPIAVAGGLDAETAAKAVAAGADIVIVGGNIIKSADVTEAARKIREAI 210
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
4-207 2.42e-15

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 73.51  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   4 PMLQVALDNQTMDsayETTRLIAE--EVD--IIEVGTILCVGEGVRAVRDLKALYPHKIVLADAKIADAGKILSRMCFEA 79
Cdd:PRK13307  173 PYLQVALDLPDLE---EVERVLSQlpKSDhiIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADA 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  80 NADWVTVICCADINTAKGALDVAKE---------FNGDVQIELtgywtWEQAQQWRDAgiqqVVYHRSRDAQAAGVAWGe 150
Cdd:PRK13307  250 TADAVVISGLAPISTIEKAIHEAQKtgiysildmLNVEDPVKL-----LESLKVKPDV----VELHRGIDEEGTEHAWG- 319

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1476721357 151 aDITAIKRLsDMGFKVTVTGGLALEDLP--LFKGIPIhvFIAGRSIRDAASPVEAARQF 207
Cdd:PRK13307  320 -NIKEIKKA-GGKILVAVAGGVRVENVEeaLKAGADI--LVVGRAITKSKDVRRAAEDF 374
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 8-207 8.09e-11

Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates orotidine 5'-monophosphate (OMP) to form uridine 5'-phosphate (UMP), an essential step in the pyrimidine biosynthetic pathway. In mammals, UMP synthase contains two domains: the orotate phosphoribosyltransferase (OPRTase) domain that catalyzes the transfer of phosphoribosyl 5'-pyrophosphate (PRPP) to orotate to form OMP, and the orotidine-5'-phosphate decarboxylase (ODCase) domain that decarboxylates OMP to form UMP.


Pssm-ID: 240076  Cd Length: 216  Bit Score: 59.11  E-value: 8.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   8 VALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALypHKIVLADAKIADAGKILSRMC---FEANADWV 84
Cdd:cd04725     3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL--GFLVFLDLKLGDIPNTVAAAAealLGLGADAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  85 TVICCADINTAKGALDVAKEFNGDVQI--ELTGyWTWEQAQQWRDAGIQQVVYHRSRDAQAAG----VAwGEADITAIKR 158
Cdd:cd04725    81 TVHPYGGSDMLKAALEAAEEKGKGLFAvtVLSS-PGALDLQEGIPGSLEDLVERLAKLAREAGvdgvVC-GATEPEALRR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721357 159 LSDMGFKVTVTG-GLALEDLPLFKGI-PIHVF-------IAGRSIRDAASPVEAARQF 207
Cdd:cd04725   159 ALGPDFLILTPGiGAQGSGDDQKRGGtPEDAIragadyiVVGRPITQAADPVAAAEAI 216
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-213 1.40e-09

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 55.76  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   1 MSLPMLQVALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALYPhkiVLADAKIADAGKILSRMC---F 77
Cdd:PRK13813    1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPNTNRLICeavF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  78 EANADWVTVICCADINTAKGALDVAKEFNGDVqieltgYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGV------AWGEA 151
Cdd:PRK13813   78 EAGAWGIIVHGFTGRDSLKAVVEAAAESGGKV------FVVVEMSHPGALEFIQPHADKLAKLAQEAGAfgvvapATRPE 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1476721357 152 DITAIKRLSDMGFKVtVTGGLALEDlplfkGIPIHVF-------IAGRSIRDAASPVEAARQFKRSIAE 213
Cdd:PRK13813  152 RVRYIRSRLGDELKI-ISPGIGAQG-----GKAADAIkagadyvIVGRSIYNAADPREAAKAINEEIRG 214
PRK00230 PRK00230
orotidine-5'-phosphate decarboxylase;
8-213 3.34e-04

orotidine-5'-phosphate decarboxylase;


Pssm-ID: 234695  Cd Length: 230  Bit Score: 40.50  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357   8 VALDNQTMDSAYETTRLIAEEVDIIEVGTILCVGEGVRAVRDLKALyPHKIVLaDAK-------IADAGKILSRMcfeaN 80
Cdd:PRK00230    7 VALDFPSKEEALAFLDQLDPAVLFVKVGMELFTAGGPQFVRELKQR-GFKVFL-DLKlhdipntVAKAVRALAKL----G 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357  81 ADWVTVICCADINTAKGALDVAKEFNGDVQI---ELTGYWTWEQAQQWRDAGIQQVVYHRSRDAQAAGV------AWgEA 151
Cdd:PRK00230   81 VDMVNVHASGGPRMMKAAREALEPKSRPLLIavtVLTSMDEEDLAELGINLSLEEQVLRLAKLAQEAGLdgvvcsAQ-EA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721357 152 diTAIKRLSDMGFKvTVTGGL------------------ALEDLPLFkgIPIhvfiaGRSIRDAASPVEAARQFKRSIAE 213
Cdd:PRK00230  160 --AAIREATGPDFL-LVTPGIrpagsdagdqkrvmtpaqAIAAGSDY--IVV-----GRPITQAADPAAAYEAILAEIAG 229
 
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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