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Conserved domains on  [gi|550766130|ref|WP_022649490|]
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MULTISPECIES: 2-hydroxy-3-oxopropionate reductase [Enterobacter]

Protein Classification

2-hydroxy-3-oxopropionate reductase( domain architecture ID 11485396)

2-hydroxy-3-oxopropionate reductase catalyzes the reduction of tatronate semialdehyde to D-glycerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-296 0e+00

tartronate semialdehyde reductase; Provisional


:

Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 553.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   1 MTLKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  81 GIIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVV 160
Cdd:PRK11559  81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766130 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEIAR 296
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
 
Name Accession Description Interval E-value
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-296 0e+00

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 553.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   1 MTLKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  81 GIIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVV 160
Cdd:PRK11559  81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766130 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEIAR 296
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 4-294 3.10e-153

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 430.08  E-value: 3.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  164 EIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 550766130  244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEI 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 2-286 9.12e-114

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 329.77  E-value: 9.12e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   2 TLKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENG 81
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  82 IIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVH 161
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 162 TGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKD 241
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 550766130 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084  241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-163 2.27e-55

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 2.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
 
Name Accession Description Interval E-value
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-296 0e+00

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 553.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   1 MTLKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  81 GIIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVV 160
Cdd:PRK11559  81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550766130 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEIAR 296
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 4-294 3.10e-153

2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60), also called tartronate semialdehyde reductase. It follows glyoxylate carboligase and precedes glycerate kinase in D-glycerate pathway of glyoxylate degradation. The eventual product, 3-phosphoglycerate, is an intermediate of glycolysis and is readily metabolized. Tartronic semialdehyde, the substrate of this enzyme, may also come from other pathways, such as D-glucarate catabolism.


Pssm-ID: 130569 [Multi-domain]  Cd Length: 291  Bit Score: 430.08  E-value: 3.10e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  164 EIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 550766130  244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEI 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 2-286 9.12e-114

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 329.77  E-value: 9.12e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   2 TLKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENG 81
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  82 IIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVH 161
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 162 TGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKD 241
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 550766130 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084  241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
3-295 4.89e-71

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 221.05  E-value: 4.89e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   3 LKVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAvAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGI 82
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  83 IDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHT 162
Cdd:PRK15059  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 163 GEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 550766130 243 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEIA 295
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 7-286 2.74e-59

3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]


Pssm-ID: 130753 [Multi-domain]  Cd Length: 288  Bit Score: 190.78  E-value: 2.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    7 FIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGIIDGA 86
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   87 KPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTGEIG 166
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  167 AGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFRIDLHI 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVpgVMPqapasNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 550766130  240 KDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-163 2.27e-55

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 2.27e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
4-282 9.72e-54

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 176.97  E-value: 9.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  84 DGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSVVHTG 163
Cdd:PRK15461  83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130 164 EIGAGNVTKLANQVI-VALNiAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKD 241
Cdd:PRK15461 163 GPGMGIRVKLINNYMsIALN-ALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKD 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 550766130 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSAL 282
Cdd:PRK15461 242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAI 282
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 166-286 1.88e-45

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 149.60  E-value: 1.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  166 GAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKDLAN 244
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 550766130  245 ALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 4-295 1.06e-32

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 127.28  E-value: 1.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PLN02858  326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEALKA--KGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSV-V 160
Cdd:PLN02858  406 SALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyV 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PLN02858  486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 550766130  241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEIA 295
Cdd:PLN02858  566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVE 620
PLN02858 PLN02858
fructose-bisphosphate aldolase
 4-294 6.97e-31

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 122.27  E-value: 6.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130    4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PLN02858    6 VVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   84 DGAKPGLVVIDMSSIAPLASREISEAL--KAKGVEMLDAPVSGGEPKAIDGTLSVMVGGDKAVFDKYYDLMKAMAGSV-V 160
Cdd:PLN02858   86 KGLQKGAVILIRSTILPLQLQKLEKKLteRKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLyT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PLN02858  166 FEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQ 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 550766130  241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEI 294
Cdd:PLN02858  246 NLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNI 299
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
4-173 1.55e-15

6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 75.13  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCD---VIITMLPNSPHVKEVaLGEn 80
Cdd:COG1023    2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQV-IEE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  81 gIIDGAKPGLVVID------MSSIAplasReiSEALKAKGVEMLDAPVSGGepkaIDGTL---SVMVGGDKAVFDKYYDL 151
Cdd:COG1023   80 -LAPLLEPGDIVIDggnsnyKDDIR----R--AEELAEKGIHFVDVGTSGG----VWGLEngyCLMIGGDKEAVERLEPI 148

                        170       180
                 ....*....|....*....|....*.
gi 550766130 152 MKAMA----GSVVHTGEIGAGNVTKL 173
Cdd:COG1023  149 FKALApgaeNGYLHCGPVGAGHFVKM 174
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
4-172 3.27e-14

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 71.32  E-value: 3.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   4 KVGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAIAEQCD---VIITMLPNSPHVKEVAlgeN 80
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI---D 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  81 GIIDGAKPGLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGepkaIDGTL---SVMVGGDKAVFDKYYDLMKAMA- 156
Cdd:PRK09599  79 ELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGG----VWGLErgyCLMIGGDKEAVERLEPIFKALAp 154

                        170
                 ....*....|....*....
gi 550766130 157 ---GSVVHTGEIGAGNVTK 172
Cdd:PRK09599 155 raeDGYLHAGPVGAGHFVK 173
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 5-192 7.08e-05

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 44.01  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130   5 VGFIGLGIMGKPMSKNLIKAGYSLVVLDRNSDAVAEVIAAGAETATTAKAiaeqCDVIITMLPNSPHVKEVAL----GE- 79
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNTRVKG----YHTLEELVNSLKKPRKVILlikaGEa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550766130  80 -NGIIDGAKP----GLVVIDMSSIAPLASREISEALKAKGVEMLDAPVSGGEPKAIDGTlSVMVGGDKAVFDKYYDLMKA 154
Cdd:PTZ00142  80 vDETIDNLLPllekGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEK 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 550766130 155 MAGSV------VHTGEIGAGNVTKLANQVIVALNIAAMSEALTL 192
Cdd:PTZ00142 159 CSAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKL 202
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 107-173 4.97e-04

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 41.24  E-value: 4.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550766130 107 SEALKAKGVEMLDAPVSGGEPKAIDGTlSVMVGGDKAVFDKYYDLMKAMAGS------VVHTGEIGAGNVTKL 173
Cdd:PLN02350 118 IKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDILEKVAAQvddgpcVTYIGPGGAGNFVKM 189
 
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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