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Conserved domains on  [gi|1327839097|ref|WP_102137519|]
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MULTISPECIES: 3-keto-L-gulonate-6-phosphate decarboxylase UlaD [Providencia]

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;
1-215 6.90e-128

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


:

Pssm-ID: 237344  Cd Length: 216  Bit Score: 359.24  E-value: 6.90e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839097 161 DLGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKGK-KTAEALREQIDRFWK 215
Cdd:PRK13306  161 DMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPaAAARAFKDEIAKYWG 216
 
Name Accession Description Interval E-value
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-215 6.90e-128

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 359.24  E-value: 6.90e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839097 161 DLGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKGK-KTAEALREQIDRFWK 215
Cdd:PRK13306  161 DMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPaAAARAFKDEIAKYWG 216
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-213 1.21e-77

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 231.98  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:COG0269     1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNW-TFEDAKNWVELGITQAIYHRSRDAELAGiGWTNEDIEKMRKL 159
Cdd:COG0269    81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAG-GSPLDDLKKIKEL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839097 160 SdlGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKG-KKTAEALREQIDRF 213
Cdd:COG0269   160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDpAAAAREIREAIDKA 212
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 4-203 2.96e-71

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: 215.52  E-value: 2.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   4 PLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAGADW 83
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  84 ITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLsdLG 163
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1327839097 164 LELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKGKKTA 203
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEA 198
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-203 3.15e-42

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: 141.63  E-value: 3.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   4 PLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKypNHILVCDMKTTDGGAILSRMA---FEAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNR-EIQIEIYGNWTFEDAKNWVELGITQAIYHRSRD--AELAGIGWTNEDIEKmR 157
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGRgLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADlaAGVDGVVASATEALR-E 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327839097 158 KLSDL-------GLELSITGGIVPEDLHLFNGIK-AKAFIAGRALVGEKGKKTA 203
Cdd:pfam00215 158 ILPDFliltpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAA 211
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-206 5.39e-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: 118.04  E-value: 5.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097    5 LIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYpNHILVCDMKTTDGGAILSRMA---FEAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVARAAraaAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   82 DWITVSAAAHIATIAACKKVADEFNR-EIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGI-----GWTneDIEK 155
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGPgLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLdgvvcSAT--EPEL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839097  156 MRKLSDLGLELSITG-GIVPEDLHLFNGIKAKA--FIAGRALVG-EKGKKTAEAL 206
Cdd:smart00934 158 IRRALGPDFLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQaADPVEAAEAI 212
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 5-213 2.06e-28

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: 105.92  E-value: 2.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   5 LIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAGADWI 84
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  85 TVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFED-AKNWVELGITQAIYHRSRDAELAGiGWTNEDIEKMRKLSdLG 163
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKrAKELKELGADYIGVHTGLDEQAKG-QNPFEDLQTILKLV-KE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327839097 164 LELSITGGIVPEDLHLFNGIKAKAFIAGRALVgeKGKKTAEALREQIDRF 213
Cdd:TIGR03128 159 ARVAVAGGINLDTIPDVIKLGPDIVIVGGAIT--KAADPAEAARQIRKLI 206
 
Name Accession Description Interval E-value
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
1-215 6.90e-128

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 359.24  E-value: 6.90e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:PRK13306    1 MSKPLLQIALDNQDLESAIEDAKKVAEEVDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLS 160
Cdd:PRK13306   81 ADWVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWTWEQAQQWRDAGISQVIYHRSRDAQLAGVAWGEKDLNKVKKLS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839097 161 DLGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKGK-KTAEALREQIDRFWK 215
Cdd:PRK13306  161 DMGFKVSVTGGLVVEDLKLFKGIPVKTFIAGRAIRGAADPaAAARAFKDEIAKYWG 216
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
1-214 1.75e-86

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 254.74  E-value: 1.75e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:PRK13305    1 MSRPLLQLALDHTSLEAAQRDVTLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLS 160
Cdd:PRK13305   81 ANWMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWTLDDARDWHRIGVRQAIYHRGRDAQASGQQWGEADLARMKALS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839097 161 DLGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEK-GKKTAEALREQIDRFW 214
Cdd:PRK13305  161 DIGLELSITGGITPADLPLFKDIRVKAFIAGRALAGAAnPAQVAADFHAQIDAIW 215
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
1-213 1.21e-77

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 231.98  E-value: 1.21e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAG 80
Cdd:COG0269     1 MMKPKLQVALDLLDLDEALAIAKEVAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNREIQIEIYGNW-TFEDAKNWVELGITQAIYHRSRDAELAGiGWTNEDIEKMRKL 159
Cdd:COG0269    81 ADIVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWdPVERAKELEELGVDIVILHRGIDAQAAG-GSPLDDLKKIKEL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839097 160 SdlGLELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKG-KKTAEALREQIDRF 213
Cdd:COG0269   160 V--GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAKDpAAAAREIREAIDKA 212
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 4-203 2.96e-71

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: 215.52  E-value: 2.96e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   4 PLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAGADW 83
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPDGVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  84 ITVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGIGWTNEDIEKMRKLsdLG 163
Cdd:cd04726    81 VTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRAKLLKLGVDIVILHRGIDAQAAGGWWPEDDLKKVKKL--LG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1327839097 164 LELSITGGIVPEDLHLFNGIKAKAFIAGRALVGEKGKKTA 203
Cdd:cd04726   159 VKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEA 198
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 4-203 3.15e-42

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: 141.63  E-value: 3.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   4 PLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKypNHILVCDMKTTDGGAILSRMA---FEAG 80
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADELGPYVDILKVGTPLFEAFGLKLVAELRKH--GFLIFLDLKFADIGNTVAKQAkykAKLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  81 ADWITVSAAAHIATIAACKKVADEFNR-EIQIEIYGNWTFEDAKNWVELGITQAIYHRSRD--AELAGIGWTNEDIEKmR 157
Cdd:pfam00215  79 ADIVTVHAYAGEGTLKAAKEAAEEYGRgLLLVAELSSKGSLDLQEEGDLGYTQEIVHRAADlaAGVDGVVASATEALR-E 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327839097 158 KLSDL-------GLELSITGGIVPEDLHLFNGIK-AKAFIAGRALVGEKGKKTA 203
Cdd:pfam00215 158 ILPDFliltpgiGLQGGDAGGQQRVTTPAVAKEAgADIIIVGRGITGAGDPVAA 211
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 5-206 5.39e-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: 118.04  E-value: 5.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097    5 LIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYpNHILVCDMKTTDGGAILSRMA---FEAGA 81
Cdd:smart00934   1 RLIVALDVPDLEEALELADALGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVARAAraaAELGA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   82 DWITVSAAAHIATIAACKKVADEFNR-EIQIEIYGNWTFEDAKNWVELGITQAIYHRSRDAELAGI-----GWTneDIEK 155
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGPgLLAVTVLTSPGAEDLQELGDESLEEQVLRLAKLAKEAGLdgvvcSAT--EPEL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1327839097  156 MRKLSDLGLELSITG-GIVPEDLHLFNGIKAKA--FIAGRALVG-EKGKKTAEAL 206
Cdd:smart00934 158 IRRALGPDFLILTPGiGDQGRVATPAVAIGAGAdiIVVGRPITQaADPVEAAEAI 212
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 5-213 2.06e-28

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: 105.92  E-value: 2.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   5 LIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEAGADWI 84
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEKVADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  85 TVSAAAHIATIAACKKVADEFNREIQIEIYGNWTFED-AKNWVELGITQAIYHRSRDAELAGiGWTNEDIEKMRKLSdLG 163
Cdd:TIGR03128  81 TVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKrAKELKELGADYIGVHTGLDEQAKG-QNPFEDLQTILKLV-KE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1327839097 164 LELSITGGIVPEDLHLFNGIKAKAFIAGRALVgeKGKKTAEALREQIDRF 213
Cdd:TIGR03128 159 ARVAVAGGINLDTIPDVIKLGPDIVIVGGAIT--KAADPAEAARQIRKLI 206
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 1-86 1.18e-21

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 91.62  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVA-ENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEA 79
Cdd:PRK07028    1 MERPILQVALDLLELDRAVEIAkEAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKA 80


                  ....*..
gi 1327839097  80 GADWITV 86
Cdd:PRK07028   81 GADIVCI 87
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
4-213 4.83e-16

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


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 75.43  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   4 PLIQIALDQTNLPAALEVAENV----HTfvdIIEVGTILAFADGMNAVSTLRQKYPNHILVCDMKTTDGGAILSRMAFEA 79
Cdd:PRK13307  173 PYLQVALDLPDLEEVERVLSQLpksdHI---IIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEARMAADA 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  80 GADWITVS----AAAHIATIAACKK-----VADEFNREIQIEIYGnwTFEDAKNWVELgitqaiyHRSRDAELAGIGWTN 150
Cdd:PRK13307  250 TADAVVISglapISTIEKAIHEAQKtgiysILDMLNVEDPVKLLE--SLKVKPDVVEL-------HRGIDEEGTEHAWGN 320

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097 151 edIEKMRKLSDLGLeLSITGGIVPEDLHlfNGIKAKA--FIAGRALVGEKGKKTA-----EALREQIDRF 213
Cdd:PRK13307  321 --IKEIKKAGGKIL-VAVAGGVRVENVE--EALKAGAdiLVVGRAITKSKDVRRAaedflNKLKPDIDQF 385
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 1-212 4.86e-09

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 54.22  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   1 MTKPLIQIALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKYPnhiLVCDMKTTD---GGAILSRMAF 77
Cdd:PRK13813    1 EKDSRIILALDVTDRERALKIAEELDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADipnTNRLICEAVF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  78 EAGADWITVSAAAHIATIAACKKVADEFNREIQI-----EIYGNWTFEDaknwvelgITQAIYHRSRDAELAGI---GWT 149
Cdd:PRK13813   78 EAGAWGIIVHGFTGRDSLKAVVEAAAESGGKVFVvvemsHPGALEFIQP--------HADKLAKLAQEAGAFGVvapATR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839097 150 NEDIEKMRKLSDLGLELsITGGIVPEDLHLFNGIKAKA--FIAGRALVG-EKGKKTAEALREQIDR 212
Cdd:PRK13813  150 PERVRYIRSRLGDELKI-ISPGIGAQGGKAADAIKAGAdyVIVGRSIYNaADPREAAKAINEEIRG 214
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 5-192 2.36e-05

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 43.73  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   5 LIQIALDQTNLPAALEVAEN-VHTFVDIIEVGTILAFADGMNAVST-----LRQKYPNHILVCDMKTTDGGA--ILSRMA 76
Cdd:cd04722     1 VILALLAGGPSGDPVELAKAaAEAGADAIIVGTRSSDPEEAETDDKevlkeVAAETDLPLGVQLAINDAAAAvdIAAAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097  77 FEAGADWITVS---AAAHIATIAACKKVADEF-NREIQIEIYGNWTFEDAKnWVELGITQAIYHRSRDAELAGIGWTNED 152
Cdd:cd04722    81 RAAGADGVEIHgavGYLAREDLELIRELREAVpDVKVVVKLSPTGELAAAA-AEEAGVDEVGLGNGGGGGGGRDAVPIAD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1327839097 153 IEKMRKLSDLGLELSITGGIV-PEDLHLFNGIKAKAFIAGR 192
Cdd:cd04722   160 LLLILAKRGSKVPVIAGGGINdPEDAAEALALGADGVIVGS 200
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 8-87 8.73e-03

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: 36.00  E-value: 8.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839097   8 IALDQTNLPAALEVAENVHTFVDIIEVGTILAFADGMNAVSTLRQKypNHILVCDMK-----TTDGGAIlsRMAFEAGAD 82
Cdd:cd04725     3 VALDPPDEEFALALIDALGPYVCAVKVGLELFEAAGPEIVKELREL--GFLVFLDLKlgdipNTVAAAA--EALLGLGAD 78


                  ....*
gi 1327839097  83 WITVS 87
Cdd:cd04725    79 AVTVH 83
 
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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