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Conserved domains on  [gi|1184523226|ref|WP_085093235|]
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NAD(P)-dependent oxidoreductase [Mycobacterium paraense]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11449905)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

CATH:  3.40.50.720
EC:  1.1.-.-
Gene Ontology:  GO:0050661|GO:0051287|GO:0016491
PubMed:  8749365
SCOP:  4000072

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-271 1.87e-62

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 198.03  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 161 GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGG---AGGLErlAGLAGTLLRK 237
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPrmlAGDFD--PGFALDLMLK 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1184523226 238 DVRLIAELAERAAADPgAVLEAAD---ATLASMGHPR 271
Cdd:COG2084   240 DLGLALEAARAAGVPL-PLAAAARqlyARAVAAGHGD 275
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-271 1.87e-62

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 198.03  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 161 GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGG---AGGLErlAGLAGTLLRK 237
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPrmlAGDFD--PGFALDLMLK 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1184523226 238 DVRLIAELAERAAADPgAVLEAAD---ATLASMGHPR 271
Cdd:COG2084   240 DLGLALEAARAAGVPL-PLAAAARqlyARAVAAGHGD 275
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-217 7.11e-34

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 124.39  E-value: 7.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGL 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHL 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184523226 161 GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNA 217
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDA 219
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 3.24e-31

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: 113.33  E-value: 3.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   2 RVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGgLL 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEG-LL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  82 GAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-219 1.04e-29

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: 113.45  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   2 RVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGLL 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  82 GAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184523226 162 DLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALG 219
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKG 218
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-271 1.87e-62

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 198.03  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGL 80
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHL 160
Cdd:COG2084    82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 161 GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGG---AGGLErlAGLAGTLLRK 237
Cdd:COG2084   162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPrmlAGDFD--PGFALDLMLK 239

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1184523226 238 DVRLIAELAERAAADPgAVLEAAD---ATLASMGHPR 271
Cdd:COG2084   240 DLGLALEAARAAGVPL-PLAAAARqlyARAVAAGHGD 275
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-217 7.11e-34

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 124.39  E-value: 7.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGL 80
Cdd:PRK11559    3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHL 160
Cdd:PRK11559   83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184523226 161 GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNA 217
Cdd:PRK11559  163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDA 219
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-161 3.24e-31

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: 113.33  E-value: 3.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   2 RVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGgLL 81
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEG-LL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  82 GAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLG 161
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-219 1.04e-29

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: 113.45  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   2 RVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGLL 81
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  82 GAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLG 161
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184523226 162 DLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALG 219
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKG 218
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 5-269 2.73e-27

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: 106.81  E-value: 2.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   5 FIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGLLGAM 84
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  85 KPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLGDLG 164
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 165 SGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGGAGGLERLA--------GLAGTLLR 236
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQApasngyqgGFGTALML 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1184523226 237 KDVRLIAELAERAAADP--GAVLEAADATLASMGH 269
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTplGALARQLYSLFDDKGH 275
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-250 1.12e-20

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 88.93  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLwarrsATLEPFADT----AARVAASPADLAAASDLVCLCVVGDADIEEITCG 76
Cdd:PRK15059    1 MKLGFIGLGIMGTPMAINLARAGHQLHV-----TTIGPVADEllslGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  77 EGGLLGAMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADP 156
Cdd:PRK15059   76 ENGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 157 VVHLGDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGgagglERL------AGL 230
Cdd:PRK15059  156 ITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHG-----ERMikrtfnPGF 230

                         250       260
                  ....*....|....*....|
gi 1184523226 231 AGTLLRKDVRLIAELAERAA 250
Cdd:PRK15059  231 KIALHQKDLNLALQSAKALA 250
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
3-176 4.07e-16

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 76.43  E-value: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   3 VGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGLLG 82
Cdd:PRK15461    4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  83 AMKPGGVIAVHSTVHPNTCRGLAKKAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVVHLGD 162
Cdd:PRK15461   84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163

                         170
                  ....*....|....
gi 1184523226 163 LGSGQTTKLLNNLL 176
Cdd:PRK15461  164 PGMGIRVKLINNYM 177
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-176 4.22e-13

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 69.11  E-value: 4.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226    2 RVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAASPADLAAASDLVCLCVVGDADIEEITCGEGGLL 81
Cdd:PLN02858   326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   82 GAMKPGGVIAVHSTVHPNTCRGLAK--KAGARGVSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPV-V 158
Cdd:PLN02858   406 SALPAGASIVLSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyV 485

                          170
                   ....*....|....*...
gi 1184523226  159 HLGDLGSGQTTKLLNNLL 176
Cdd:PLN02858   486 IKGGCGAGSGVKMVNQLL 503
PLN02858 PLN02858
fructose-bisphosphate aldolase
 3-212 1.07e-12

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 67.95  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226    3 VGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAA-RVAASPADLAAASDLVclCVVGDAD-IEEITCGEGGL 80
Cdd:PLN02858     7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGhRCDSPAEAAKDAAALV--VVLSHPDqVDDVFFGDEGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   81 LGAMKPGGVIAVHSTVHPNTCRGLAKKAGARG--VSVVDAPVSGGGGAASEGRLLVMVGGDADVVGRCRPVFETYADPVV 158
Cdd:PLN02858    85 AKGLQKGAVILIRSTILPLQLQKLEKKLTERKeqIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLY 164

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1184523226  159 HL-GDLGSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANS 212
Cdd:PLN02858   165 TFeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSS 219
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 164-249 6.19e-08

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: 50.22  E-value: 6.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226 164 GSGQTTKLLNNLLFTANLGTAAAALSLADALGVSPDRFTEVASRGSANSFALNALGGAGGLERL--AGLAGTLLRKDVRL 241
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQRVLSRDfdPGFALDLMLKDLGL 80


                  ....*...
gi 1184523226 242 IAELAERA 249
Cdd:pfam14833  81 ALDLARAL 88
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-174 5.75e-07

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 49.70  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAARVAaspadlaaaSDLVCLC-------VV------G- 66
Cdd:COG1023     1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGA---------DSLEELVaklpaprVVwlmvpaGe 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  67 --DADIEEitcgeggLLGAMKPGGVIA-------VHSTVHpntcrglAKKAGARGVSVVDAPVSGGggaasegrllV--- 134
Cdd:COG1023    72 itDQVIEE-------LAPLLEPGDIVIdggnsnyKDDIRR-------AEELAEKGIHFVDVGTSGG----------Vwgl 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184523226 135 ------MVGGDADVVGRCRPVFETYADPV----VHLGDLGSGQTTKLLNN 174
Cdd:COG1023   128 engyclMIGGDKEAVERLEPIFKALAPGAengyLHCGPVGAGHFVKMVHN 177
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-174 2.67e-05

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 44.74  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226   1 MRVGFIGLGSQGGPMARRIVEAGYETTLWARRSATLEPFADTAArvaaspadlaaasdlvclcvVGDADIEEITcgegGL 80
Cdd:PRK09599    1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGA--------------------TGADSLEELV----AK 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184523226  81 LGA------MKPGGVIaVHSTVH---PNTCRG----------------LAKKAGARGVSVVDAPVSGGGGAASEGRLLvM 135
Cdd:PRK09599   57 LPAprvvwlMVPAGEI-TDATIDelaPLLSPGdividggnsyykddirRAELLAEKGIHFVDVGTSGGVWGLERGYCL-M 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1184523226 136 VGGDADVVGRCRPVFETYADPV----VHLGDLGSGQTTKLLNN 174
Cdd:PRK09599  135 IGGDKEAVERLEPIFKALAPRAedgyLHAGPVGAGHFVKMVHN 177
 
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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