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Conserved domains on  [gi|2286513913|ref|WP_257784246|]
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2-hydroxy-3-oxopropionate reductase [Serratia plymuthica]

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
 14-307 0e+00

tartronate semialdehyde reductase; Provisional


:

Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEVSR 307
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
 
Name Accession Description Interval E-value
garR PRK11559
tartronate semialdehyde reductase; Provisional
 14-307 0e+00

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEVSR 307
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 15-305 3.22e-151

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: 425.46  E-value: 3.22e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGII 94
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTG 174
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 175 EIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDLA 254
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2286513913 255 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEV 305
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 14-297 1.46e-125

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 359.81  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYY 297
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 15-174 7.72e-64

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: 198.46  E-value: 7.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGkDGII 94
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTG 174
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 15-127 7.50e-04

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 40.73  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVaEQSDILITMLPNSPQVQEvaLGKDGII 94
Cdd:cd12157   146 TVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELL-ESSDFLVLALPLTPDTLH--LINAEAL 222

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIA 127
Cdd:cd12157   223 AKMKPGALLVNPCRGSVVDEAAVAEALKSGHLG 255
 
Name Accession Description Interval E-value
garR PRK11559
tartronate semialdehyde reductase; Provisional
 14-307 0e+00

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 561.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEVSR 307
Cdd:PRK11559  243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 15-305 3.22e-151

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: 425.46  E-value: 3.22e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGII 94
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTG 174
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 175 EIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDLA 254
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2286513913 255 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEV 305
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 14-297 1.46e-125

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 359.81  E-value: 1.46e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYY 297
Cdd:COG2084   242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
14-306 3.45e-79

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 242.62  E-value: 3.45e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPqTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGI 93
Cdd:PRK15059    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  94 IEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHT 173
Cdd:PRK15059   80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 174 GEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIKDL 253
Cdd:PRK15059  160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2286513913 254 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEVS 306
Cdd:PRK15059  240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 18-297 2.13e-64

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: 204.26  E-value: 2.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  18 FIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGIIEGA 97
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  98 RPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTGEIG 177
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 178 AGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFRIELHI 250
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVpgVMPqapasNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2286513913 251 KDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYY 297
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 15-174 7.72e-64

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: 198.46  E-value: 7.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGkDGII 94
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTG 174
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
15-293 3.44e-59

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 191.22  E-value: 3.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGII 94
Cdd:PRK15461    3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSVVHTG 174
Cdd:PRK15461   83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 175 EIGAGNVTKLANQVI-VALNiAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIELHIKD 252
Cdd:PRK15461  163 GPGMGIRVKLINNYMsIALN-ALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKD 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2286513913 253 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSAL 293
Cdd:PRK15461  242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAI 282
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 177-297 2.92e-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: 2.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913 177 GAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIELHIKDLAN 255
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2286513913 256 ALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYY 297
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PLN02858 PLN02858
fructose-bisphosphate aldolase
 8-305 2.96e-38

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 143.84  E-value: 2.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913    8 CKEVNlmKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVA 87
Cdd:PLN02858   321 AKPVK--RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVL 398

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913   88 LGKDGIIEGARPGSVLVDMSSIAPLASREISAALAE--KQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKA 165
Cdd:PLN02858   399 FGDLGAVSALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSA 478

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  166 MAGSV-VHTGEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGF 244
Cdd:PLN02858   479 LSEKLyVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYS 558

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2286513913  245 RIELHIKDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEV 305
Cdd:PLN02858   559 ALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKV 619
PLN02858 PLN02858
fructose-bisphosphate aldolase
 15-306 8.61e-38

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 142.68  E-value: 8.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913   15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSDILITMLPNSPQVQEVALGKDGII 94
Cdd:PLN02858     6 VVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913   95 EGARPGSVLVDMSSIAPLASREISAALAE--KQIAMLDAPVSGGEPKAIDATLSVMVGGDKAVFERCLPVMKAMAGSV-V 171
Cdd:PLN02858    86 KGLQKGAVILIRSTILPLQLQKLEKKLTErkEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLyT 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  172 HTGEIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIELHIK 251
Cdd:PLN02858   166 FEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQ 245

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2286513913  252 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGASDHSALACYYEKLAKAEVS 306
Cdd:PLN02858   246 NLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNIL 300
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
14-184 1.19e-25

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 103.25  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSD---ILITMLPNSPQVQEVAlgk 90
Cdd:COG1023     1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQVI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  91 DGIIEGARPGSVLVD------MSSIAplasReiSAALAEKQIAMLDAPVSGGePKAIDATLSVMVGGDKAVFERCLPVMK 164
Cdd:COG1023    78 EELAPLLEPGDIVIDggnsnyKDDIR----R--AEELAEKGIHFVDVGTSGG-VWGLENGYCLMIGGDKEAVERLEPIFK 150

                         170       180
                  ....*....|....*....|....
gi 2286513913 165 AMA----GSVVHTGEIGAGNVTKL 184
Cdd:COG1023   151 ALApgaeNGYLHCGPVGAGHFVKM 174
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
14-183 2.46e-24

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 99.82  E-value: 2.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVAEQSD---ILITMLPNSPQVQEVAlgk 90
Cdd:PRK09599    1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  91 DGIIEGARPGSVLVD------MSSIAplasReiSAALAEKQIAMLDAPVSGGePKAIDATLSVMVGGDKAVFERCLPVMK 164
Cdd:PRK09599   78 DELAPLLSPGDIVIDggnsyyKDDIR----R--AELLAEKGIHFVDVGTSGG-VWGLERGYCLMIGGDKEAVERLEPIFK 150

                         170       180
                  ....*....|....*....|...
gi 2286513913 165 AMA----GSVVHTGEIGAGNVTK 183
Cdd:PRK09599  151 ALApraeDGYLHAGPVGAGHFVK 173
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 14-74 4.96e-07

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 50.06  E-value: 4.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYS---LVVLNHHPQTTAELVA-LGATAAETPKAVAEQSDILI 74
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVV 67
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 14-74 1.38e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 45.52  E-value: 1.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYS---LVVLNHHPQTTAELVA-LGATAAETPKAVAEQSDILI 74
Cdd:PRK11880    3 KKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEeYGVRAATDNQEAAQEADVVV 67
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 14-109 1.04e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 43.44  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  14 MKIGFIG-LGIMGKPMSKNLLKAGYSLVVLNHHPQTTAElVA--LGATAAETPKAVAEQSDILITMLPNSpqVQEvalgk 90
Cdd:PRK08655    1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKE-VAkeLGVEYANDNIDAAKDADIVIISVPIN--VTE----- 72

                          90       100
                  ....*....|....*....|..
gi 2286513913  91 DGIIEGA---RPGSVLVDMSSI 109
Cdd:PRK08655   73 DVIKEVAphvKEGSLLMDVTSV 94
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 15-210 1.26e-04

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 43.16  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETP-----------KAVAEQSDILITMLPNSPQV 83
Cdd:PLN02350    8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLPlygfkdpedfvLSIQKPRSVIILVKAGAPVD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  84 QEValgkDGIIEGARPGSVLVDMSSIAPLASREISAALAEKQIAMLDAPVSGGEPKAIDATlSVMVGGDKAVFERCLPVM 163
Cdd:PLN02350   88 QTI----KALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDIL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2286513913 164 KAMAGS------VVHTGEIGAGNVTKLANQVIVALNIAAMSEAL-VLATKAGVN 210
Cdd:PLN02350  163 EKVAAQvddgpcVTYIGPGGAGNFVKMVHNGIEYGDMQLISEAYdVLKSVGGLS 216
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 14-74 1.70e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 42.49  E-value: 1.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2286513913  14 MKIGFIGLGIMGKPMSKNLLKAGYSLV-VLNHHPQTTAELVA-LGATAAETPKAVAEQSDILI 74
Cdd:COG5495     4 MKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAAlLGAVPALDLEELAAEADLVL 66
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 15-127 7.50e-04

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 40.73  E-value: 7.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2286513913  15 KIGFIGLGIMGKPMSKNLLKAGYSLVVLNHHPQTTAELVALGATAAETPKAVaEQSDILITMLPNSPQVQEvaLGKDGII 94
Cdd:cd12157   146 TVGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVELDELL-ESSDFLVLALPLTPDTLH--LINAEAL 222

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2286513913  95 EGARPGSVLVDMSSIAPLASREISAALAEKQIA 127
Cdd:cd12157   223 AKMKPGALLVNPCRGSVVDEAAVAEALKSGHLG 255
 
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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