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Conserved domains on  [gi|16130643|ref|NP_417216|]
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putative L-threonate dehydrogenase [Escherichia coli str. K-12 substr. MG1655]

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

 Zoom to residue level

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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 ...
 8-292 1.51e-79

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 242.71  E-value: 1.51e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   8 HVGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGAcGVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGV 87
Cdd:COG2084   3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGA-RVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  88 AQHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRI 167
Cdd:COG2084  82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643 168 GaEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKD 247
Cdd:COG2084 162 G-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 16130643 248 LGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 8-292 1.51e-79

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 242.71  E-value: 1.51e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   8 HVGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGAcGVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGV 87
Cdd:COG2084   3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGA-RVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  88 AQHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRI 167
Cdd:COG2084  82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643 168 GaEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKD 247
Cdd:COG2084 162 G-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 16130643 248 LGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PLN02858 PLN02858
fructose-bisphosphate aldolase
 9-301 9.71e-74

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 245.92  E-value: 9.71e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643     9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACgVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGVA 88
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGL-AGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    89 QHLKPGTAVMVSSTIASADAQEIATAL--AGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYR 166
Cdd:PLN02858  406 SALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYV 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   167 IGAEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVK 246
Cdd:PLN02858  486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16130643   247 DLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIFSgiTLPGAK 301
Cdd:PLN02858  566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYE--TLTGVK 618
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 9-168 2.82e-43

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: 145.69  E-value: 2.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643     9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACGVSDnAATFAEKLDALLVLVVNAAQVKQVLFGEtGVA 88
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAS-PAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    89 QHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIG 168
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 12-292 1.29e-37

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: 134.93  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    12 VGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGaCGVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGVAQHL 91
Cdd:TIGR01692   2 IGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAG-AQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    92 KPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIGAEp 171
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDH- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   172 GLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFE--NRMRHVVDG-----DYTPHSAVDIF 244
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 16130643   245 VKDLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 8-292 1.51e-79

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 242.71  E-value: 1.51e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   8 HVGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGAcGVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGV 87
Cdd:COG2084   3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGA-RVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  88 AQHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRI 167
Cdd:COG2084  82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643 168 GaEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKD 247
Cdd:COG2084 162 G-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 16130643 248 LGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PLN02858 PLN02858
fructose-bisphosphate aldolase
 9-301 9.71e-74

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 245.92  E-value: 9.71e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643     9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACgVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGVA 88
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGL-AGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    89 QHLKPGTAVMVSSTIASADAQEIATAL--AGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYR 166
Cdd:PLN02858  406 SALPAGASIVLSSTVSPGFVIQLERRLenEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYV 485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   167 IGAEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVK 246
Cdd:PLN02858  486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16130643   247 DLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIFSgiTLPGAK 301
Cdd:PLN02858  566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYE--TLTGVK 618
PLN02858 PLN02858
fructose-bisphosphate aldolase
 9-291 9.93e-59

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 202.77  E-value: 9.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643     9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGacGVSDNAATFAEKLDALLVLVV-NAAQVKQVLFGETGV 87
Cdd:PLN02858    7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELG--GHRCDSPAEAAKDAAALVVVLsHPDQVDDVFFGDEGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    88 AQHLKPGTAVMVSSTIASADAQEIATALA--GFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVY 165
Cdd:PLN02858   85 AKGLQKGAVILIRSTILPLQLQKLEKKLTerKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLY 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   166 RIGAEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFV 245
Cdd:PLN02858  165 TFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLV 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 16130643   246 KDLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKI 291
Cdd:PLN02858  245 QNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKV 290
garR PRK11559
tartronate semialdehyde reductase; Provisional
 9-292 7.78e-50

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 167.15  E-value: 7.78e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACGVSdNAATFAEKLDALLVLVVNAAQVKQVLFGETGVA 88
Cdd:PRK11559   5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETAS-TAKAVAEQCDVIITMLPNSPHVKEVALGENGII 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   89 QHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIG 168
Cdd:PRK11559  84 EGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  169 aEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKDL 248
Cdd:PRK11559 164 -DIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 16130643  249 GLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 9-168 2.82e-43

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: 145.69  E-value: 2.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643     9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACGVSDnAATFAEKLDALLVLVVNAAQVKQVLFGEtGVA 88
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAAS-PAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    89 QHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIG 168
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 12-292 1.29e-37

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: 134.93  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    12 VGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGaCGVSDNAATFAEKLDALLVLVVNAAQVKQVLFGETGVAQHL 91
Cdd:TIGR01692   2 IGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAG-AQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    92 KPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIGAEp 171
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDH- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   172 GLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFE--NRMRHVVDG-----DYTPHSAVDIF 244
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 16130643   245 VKDLGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIKIF 292
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
9-296 1.88e-35

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 129.59  E-value: 1.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACGVSdNAATFAEKLDALLVLVVNAAQVKQVLFGETGVA 88
Cdd:PRK15461   4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAA-SPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   89 QHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIG 168
Cdd:PRK15461  83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  169 aEPGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVT-NAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKD 247
Cdd:PRK15461 163 -GPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSgTAAGKGHFTTTWPNKVLKGDLSPAFMIDLAHKD 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16130643  248 LGLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAV---IKIFSGIT 296
Cdd:PRK15461 242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIleqVRVSAGLT 293
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
9-290 3.19e-26

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 104.72  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    9 VGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKeAGACGVsDNAATFAEKLDALLVLVVNAAQVKQVLFGETGVA 88
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLS-LGAVSV-ETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   89 QHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGEMTVMASGSDIAFERLAPVLEAVAGKVYRIG 168
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643  169 AEpGLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRMRHVVDGDYTPHSAVDIFVKDL 248
Cdd:PRK15059 161 GN-GDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 16130643  249 GLVADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIK 290
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQ 281
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 172-290 1.84e-25

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: 97.98  E-value: 1.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   172 GLGSTVKIIHQLLAGVHIAAGAEAMALAARAGIPLDVMYDVVTNAAGNSWMFENRM-RHVVDGDYTPHSAVDIFVKDLGL 250
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFpQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 16130643   251 VADTAKALHFPLPLASTALNMFTSASNAGYGKEDDSAVIK 290
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIR 120
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
8-181 1.02e-10

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 61.30  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643    8 HVGIVGLGSMGMGAALSYVRAGLSTWGADLNSNACATLKEAGACGVSDNAAtFAEKLDA---LLVLVVNAAQVKQVLfge 84
Cdd:PRK09599   2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEE-LVAKLPAprvVWLMVPAGEITDATI--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   85 TGVAQHLKPGTAVMVSSTIASADAQEIATALAGFDLEMLDAPVSGGAVKAANGeMTVMASGSDIAFERLAPVLEAVA--- 161
Cdd:PRK09599  78 DELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKALApra 156

                        170       180
                 ....*....|....*....|..
gi 16130643  162 --GKVYrIGaEPGLGSTVKIIH 181
Cdd:PRK09599 157 edGYLH-AG-PVGAGHFVKMVH 176
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 8-118 2.88e-04

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 41.65  E-value: 2.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130643   8 HVGIVGLGSMG--MGAALSYVRAGLSTWGADLNSNACATLKEAGAC-GVSDNAATFAEKLDallvLVVNAAQVKQV--LF 82
Cdd:COG0287   3 RIAIIGLGLIGgsLALALKRAGLAHEVVGVDRSPETLERALELGVIdRAATDLEEAVADAD----LVVLAVPVGATieVL 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16130643  83 GEtgVAQHLKPGTAVM-VSSTIAS--ADAQEIATALAGF 118
Cdd:COG0287  79 AE--LAPHLKPGAIVTdVGSVKGAvvEAAEALLPDGVRF 115
 
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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