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Conserved domains on  [gi|2315625602|dbj|GIX08248|]
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MAG: D-arabino 3-hexulose 6-phosphate aldehyde lyase [Candidatus Poribacteria bacterium]

Protein Classification

SgbH family protein( domain architecture ID 10000825)

SgbH family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
12-207 7.51e-69

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


:

Pssm-ID: 440039  Cd Length: 212  Bit Score: 210.79  E-value: 7.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKE-VAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEDPslSPLDELEAVFWAT 171
Cdd:COG0269    83 IVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGG--SPLDDLKKIKELV 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLVIDA 207
Cdd:COG0269   161 GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAK 196
 
Name Accession Description Interval E-value
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
12-207 7.51e-69

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 210.79  E-value: 7.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKE-VAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEDPslSPLDELEAVFWAT 171
Cdd:COG0269    83 IVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGG--SPLDDLKKIKELV 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLVIDA 207
Cdd:COG0269   161 GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAK 196
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 12-213 1.91e-63

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: 196.65  E-value: 1.91e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAAVRaGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPD-GVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAArQMEQFGVDVLLVHTSYDARNEDPSlSPLDELEAVFWAT 171
Cdd:cd04726    80 IVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRA-KLLKLGVDIVILHRGIDAQAAGGW-WPEDDLKKVKKLL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLVIDAHAFRPA 213
Cdd:cd04726   158 GVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 12-204 2.50e-59

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 193.31  E-value: 2.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAAVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:PRK07028    4 PILQVALDLLELDRAVEIAKEAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEdpSLSPLDELEAVFWAT 171
Cdd:PRK07028   84 IVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQML--GKDPLELLKEVSEEV 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLV 204
Cdd:PRK07028  162 SIPIAVAGGLDAETAAKAVAAGADIVIVGGNII 194
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 13-223 2.95e-48

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: 157.92  E-value: 2.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  13 IVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGASW 92
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEK-VADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  93 VVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEDPslSPLDELEAVFWATK 172
Cdd:TIGR03128  80 VTVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQ--NPFEDLQTILKLVK 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315625602 173 LPLQAV-GGLSPEQAVRMPTLGAPLVVLGAPLvidAHAFRPATSGEELEALL 223
Cdd:TIGR03128 158 EARVAVaGGINLDTIPDVIKLGPDIVIVGGAI---TKAADPAEAARQIRKLI 206
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 14-137 2.96e-25

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: 98.78  E-value: 2.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602   14 VQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFpDRAIVADAKIMDGGYLE---AELLAQAGA 90
Cdd:smart00934   2 LIVALDVPDLEEALELADA-LGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVaraARAAAELGA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2315625602   91 SWVVVMAVAHPATVRAVVRAGQRYGVGVMA-DLMAAPDPVDAARQMEQ 137
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGPGLLAvTVLTSPGAEDLQELGDE 127
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 12-151 9.93e-25

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: 97.33  E-value: 9.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDraIVADAKIMDGGYLE---AELLAQA 88
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADE-LGPYVDILKVGTPLFEAFGLKLVAELRKHGFL--IFLDLKFADIGNTVakqAKYKAKL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315625602  89 GASWVVVMAVAHPATVRAVVRAGQRYGVGVMA-DLMAAPDPVDAArQMEQFGVDVLLVHTSYDA 151
Cdd:pfam00215  78 GADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLvAELSSKGSLDLQ-EEGDLGYTQEIVHRAADL 140
 
Name Accession Description Interval E-value
UlaD COG0269
3-keto-L-gulonate-6-phosphate decarboxylase [Carbohydrate transport and metabolism];
12-207 7.51e-69

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


Pssm-ID: 440039  Cd Length: 212  Bit Score: 210.79  E-value: 7.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:COG0269     4 PKLQVALDLLDLDEALAIAKE-VAGGVDIIEAGTPLIKSEGMRAVRELRAAFPDKIIVADLKTMDAGALEAEMAFKAGAD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEDPslSPLDELEAVFWAT 171
Cdd:COG0269    83 IVTVLGAADDATIKGAVKAAKKYGKEVQVDLIGVWDPVERAKELEELGVDIVILHRGIDAQAAGG--SPLDDLKKIKELV 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLVIDA 207
Cdd:COG0269   161 GVPVAVAGGINPETLPEFLGAGADIVIVGRAITGAK 196
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 12-213 1.91e-63

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: 196.65  E-value: 1.91e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAAVRaGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:cd04726     1 PLLQVALDLLDLEEALELAKKVPD-GVDIIEAGTPLIKSEGMEAVRALREAFPDKIIVADLKTADAGALEAEMAFKAGAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAArQMEQFGVDVLLVHTSYDARNEDPSlSPLDELEAVFWAT 171
Cdd:cd04726    80 IVTVLGAAPLSTIKKAVKAAKKYGKEVQVDLIGVEDPEKRA-KLLKLGVDIVILHRGIDAQAAGGW-WPEDDLKKVKKLL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLVIDAHAFRPA 213
Cdd:cd04726   158 GVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAA 199
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
 12-204 2.50e-59

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


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 193.31  E-value: 2.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAAVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:PRK07028    4 PILQVALDLLELDRAVEIAKEAVAGGADWIEAGTPLIKSEGMNAIRTLRKNFPDHTIVADMKTMDTGAIEVEMAAKAGAD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEdpSLSPLDELEAVFWAT 171
Cdd:PRK07028   84 IVCILGLADDSTIEDAVRAARKYGVRLMADLINVPDPVKRAVELEELGVDYINVHVGIDQQML--GKDPLELLKEVSEEV 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2315625602 172 KLPLQAVGGLSPEQAVRMPTLGAPLVVLGAPLV 204
Cdd:PRK07028  162 SIPIAVAGGLDAETAAKAVAAGADIVIVGGNII 194
RuMP_HxlA TIGR03128
3-hexulose-6-phosphate synthase; Members of this protein family are 3-hexulose-6-phosphate ...
 13-223 2.95e-48

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: 157.92  E-value: 2.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  13 IVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGASW 92
Cdd:TIGR03128   1 KLQLALDLLDIEEALELAEK-VADYVDIIEIGTPLIKNEGIEAVKEMKEAFPDRKVLADLKTMDAGEYEAEQAFAAGADI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  93 VVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGVDVLLVHTSYDARNEDPslSPLDELEAVFWATK 172
Cdd:TIGR03128  80 VTVLGVADDATIKGAVKAAKKHGKEVQVDLINVKDKVKRAKELKELGADYIGVHTGLDEQAKGQ--NPFEDLQTILKLVK 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315625602 173 LPLQAV-GGLSPEQAVRMPTLGAPLVVLGAPLvidAHAFRPATSGEELEALL 223
Cdd:TIGR03128 158 EARVAVaGGINLDTIPDVIKLGPDIVIVGGAI---TKAADPAEAARQIRKLI 206
ulaD PRK13306
3-dehydro-L-gulonate-6-phosphate decarboxylase;
12-151 9.69e-30

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


Pssm-ID: 237344  Cd Length: 216  Bit Score: 110.40  E-value: 9.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAAVRAgVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:PRK13306    4 PLLQIALDNQDLESAIEDAKKVAEE-VDIIEVGTILLLAEGMKAVRVLRALYPDKIIVADTKIADAGKILAKMAFEAGAD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDpVDAARQMEQFGVDVLLVHTSYDA 151
Cdd:PRK13306   83 WVTVICAAHIPTIKAALKVAKEFNGEIQIELYGNWT-WEQAQQWRDAGISQVIYHRSRDA 141
OMPdecase smart00934
Orotidine 5'-phosphate decarboxylase / HUMPS family; Orotidine 5'-phosphate decarboxylase ...
 14-137 2.96e-25

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: 98.78  E-value: 2.96e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602   14 VQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFpDRAIVADAKIMDGGYLE---AELLAQAGA 90
Cdd:smart00934   2 LIVALDVPDLEEALELADA-LGDSVDIIKVGTELFLAEGPEGVKELKELF-GFPVFLDLKLHDIPNTVaraARAAAELGA 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2315625602   91 SWVVVMAVAHPATVRAVVRAGQRYGVGVMA-DLMAAPDPVDAARQMEQ 137
Cdd:smart00934  80 DAVTVHAYAGSDMIEAALEAAKKYGPGLLAvTVLTSPGAEDLQELGDE 127
OMPdecase pfam00215
Orotidine 5'-phosphate decarboxylase / HUMPS family; This family includes Orotidine 5 ...
 12-151 9.93e-25

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: 97.33  E-value: 9.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDraIVADAKIMDGGYLE---AELLAQA 88
Cdd:pfam00215   1 PNLCVALDVPTLEEALELADE-LGPYVDILKVGTPLFEAFGLKLVAELRKHGFL--IFLDLKFADIGNTVakqAKYKAKL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2315625602  89 GASWVVVMAVAHPATVRAVVRAGQRYGVGVMA-DLMAAPDPVDAArQMEQFGVDVLLVHTSYDA 151
Cdd:pfam00215  78 GADIVTVHAYAGEGTLKAAKEAAEEYGRGLLLvAELSSKGSLDLQ-EEGDLGYTQEIVHRAADL 140
sgbH PRK13305
3-keto-L-gulonate-6-phosphate decarboxylase UlaD;
12-151 2.11e-19

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


Pssm-ID: 183962  Cd Length: 218  Bit Score: 83.32  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  12 PIVQISLDLTSLDEAIAYAeAAVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEAELLAQAGAS 91
Cdd:PRK13305    4 PLLQLALDHTSLEAAQRDV-TLLKDHVDIVEAGTILCLNEGLGAVKALREQCPDKIIVADWKVADAGETLAQQAFGAGAN 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDpVDAARQMEQFGVDVLLVHTSYDA 151
Cdd:PRK13305   83 WMTIICAAPLATVEKGHAVAQRCGGEIQIELFGNWT-LDDARDWHRIGVRQAIYHRGRDA 141
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
7-200 3.32e-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: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602   7 FRV----DEPIVQISLDLTSLDEAIAYAEAAVRAGVDWLEVGTPLLLSEGCRAVAALRERFPDRAIVADAKIMDGGYLEA 82
Cdd:PRK13307  164 FKVtrlwDPPYLQVALDLPDLEEVERVLSQLPKSDHIIIEAGTPLIKKFGLEVISKIREVRPDAFIVADLKTLDTGNLEA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  83 ELLAQAGASWVVVMAVAHPATVRAVVRAGQRYGVGVMADLMAAPDPVDAARQMEQFGvDVLLVHTSYDARNEDPSLSPLD 162
Cdd:PRK13307  244 RMAADATADAVVISGLAPISTIEKAIHEAQKTGIYSILDMLNVEDPVKLLESLKVKP-DVVELHRGIDEEGTEHAWGNIK 322

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2315625602 163 ELEAVfwATKLPLQAVGGLSPEQAVRMPTLGAPLVVLG 200
Cdd:PRK13307  323 EIKKA--GGKILVAVAGGVRVENVEEALKAGADILVVG 358
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 21-125 5.13e-05

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 42.89  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  21 TSLDEAIAYAEAAVRAGVDWLEVgtPLLLSEGCRAVAALRERFPDrAIVADAKIMDGGylEAELLAQAGASWvVVMAVAH 100
Cdd:cd00452    13 DDAEDALALAEALIEGGIRAIEI--TLRTPGALEAIRALRKEFPE-ALIGAGTVLTPE--QADAAIAAGAQF-IVSPGLD 86

                          90       100
                  ....*....|....*....|....*..
gi 2315625602 101 PATVRAVVRAGQRYGVGVM--ADLMAA 125
Cdd:cd00452    87 PEVVKAANRAGIPLLPGVAtpTEIMQA 113
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 81-200 2.34e-04

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 41.02  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  81 EAELLAQAGASWVVVMAVAHPATVRA-----VVRAGQRYGVGVMADLmaapDPVDAARQMEQFGVDV----LLVHTSYDA 151
Cdd:cd04729    84 EVDALAAAGADIIALDATDRPRPDGEtlaelIKRIHEEYNCLLMADI----STLEEALNAAKLGFDIigttLSGYTEETA 159

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2315625602 152 RNEDPSLSPLDELEAvfwATKLPLQAVGGL-SPEQAVRMPTLGAPLVVLG 200
Cdd:cd04729   160 KTEDPDFELLKELRK---ALGIPVIAEGRInSPEQAAKALELGADAVVVG 206
PRK13813 PRK13813
orotidine 5'-phosphate decarboxylase; Provisional
 16-115 2.64e-04

orotidine 5'-phosphate decarboxylase; Provisional


Pssm-ID: 237520  Cd Length: 215  Bit Score: 40.74  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  16 ISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRERFPdraIVADAKIMDGGY---LEAELLAQAGASW 92
Cdd:PRK13813    8 LALDVTDRERALKIAEE-LDDYVDAIKVGWPLVLASGLGIIEELKRYAP---VIADLKVADIPNtnrLICEAVFEAGAWG 83

                          90       100
                  ....*....|....*....|...
gi 2315625602  93 VVVMAVAHPATVRAVVRAGQRYG 115
Cdd:PRK13813   84 IIVHGFTGRDSLKAVVEAAAESG 106
OMP_decarboxylase_like cd04725
Orotidine 5'-phosphate decarboxylase (ODCase) is a dimeric enzyme that decarboxylates ...
 16-120 3.98e-04

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: 40.24  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  16 ISLDLTSLDEAIAYAEAaVRAGVDWLEVGTPLLLSEGCRAVAALRER-FPdraIVADAKIMDGGY---LEAELLAQAGAS 91
Cdd:cd04725     3 VALDPPDEEFALALIDA-LGPYVCAVKVGLELFEAAGPEIVKELRELgFL---VFLDLKLGDIPNtvaAAAEALLGLGAD 78

                          90       100
                  ....*....|....*....|....*....
gi 2315625602  92 WVVVMAVAHPATVRAVVRAGQRYGVGVMA 120
Cdd:cd04725    79 AVTVHPYGGSDMLKAALEAAEEKGKGLFA 107
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 24-121 6.47e-03

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 37.37  E-value: 6.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2315625602  24 DEAIAYAEAAVRAGVDWLEVGTPLLLSEGC-RAVAALRERFPDRAI----VADAkimDGgyleAELLAQAGASWV----- 93
Cdd:pfam00478 219 DDTLERAEALVEAGVDVLVVDTAHGHSKGViDTVKWIKKKYPDVQViagnVATA---EG----AKALIEAGADAVkvgig 291

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2315625602  94 --------VVMAVAHP-AT-VRAVVRAGQRYGVGVMAD 121
Cdd:pfam00478 292 pgsicttrVVAGVGVPqLTaIYDVAEAAKKYGVPVIAD 329
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 170-220 6.55e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 37.19  E-value: 6.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2315625602 170 ATKLPLQAVGGL-SPEQAVRMPTLGAPLVVLGAPLVIDAHAFRPATSGEELE 220
Cdd:cd04735   282 AGRLPLIAVGSInTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEGREDE 333
 
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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