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Conserved domains on  [gi|694110399|ref|WP_032452756|]
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MULTISPECIES: L-threonate dehydrogenase [Klebsiella]

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 ...
 5-290 1.75e-76

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 235.01  E-value: 1.75e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   5 TNVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESG 84
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVA-ASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  85 LAGHLKPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYR 164
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 165 IGsDIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVK 244
Cdd:COG2084  161 VG-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 694110399 245 DLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-290 1.75e-76

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 235.01  E-value: 1.75e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   5 TNVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESG 84
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVA-ASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  85 LAGHLKPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYR 164
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 165 IGsDIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVK 244
Cdd:COG2084  161 VG-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 694110399 245 DLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PLN02858 PLN02858
fructose-bisphosphate aldolase
 10-294 8.58e-66

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 223.19  E-value: 8.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKgAGPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:PLN02858  330 IGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGL-AGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVSAL 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   90 KPGTAVMVSSTIASADAQAIAA--ALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGS 167
Cdd:PLN02858  409 PAGASIVLSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYVIKG 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  168 DIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVKDLG 247
Cdd:PLN02858  489 GCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVKDLG 568

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 694110399  248 LVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIFNGIT 294
Cdd:PLN02858  569 IVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLT 615
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 6-166 4.79e-41

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: 139.91  E-value: 4.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399    6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGEsGL 85
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAA-ASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   86 AGHLKPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRI 165
Cdd:pfam03446  79 LPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYI 158


                  .
gi 694110399  166 G 166
Cdd:pfam03446 159 G 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 10-290 4.15e-36

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: 131.07  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:TIGR01692   2 IGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAA-ASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   90 KPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGsDI 169
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCG-DH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFE--NRMQHVLDG-----DYSPKSAVDIF 242
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 694110399  243 VKDLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-51 3.99e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.07  E-value: 3.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 694110399   6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGA 51
Cdd:cd05188  137 TVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHV 182
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-290 1.75e-76

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 235.01  E-value: 1.75e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   5 TNVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESG 84
Cdd:COG2084    2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVA-ASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  85 LAGHLKPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYR 164
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 165 IGsDIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVK 244
Cdd:COG2084  161 VG-DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 694110399 245 DLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
PLN02858 PLN02858
fructose-bisphosphate aldolase
 10-294 8.58e-66

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 223.19  E-value: 8.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKgAGPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:PLN02858  330 IGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGL-AGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVSAL 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   90 KPGTAVMVSSTIASADAQAIAA--ALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGS 167
Cdd:PLN02858  409 PAGASIVLSSTVSPGFVIQLERrlENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLYVIKG 488

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  168 DIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVKDLG 247
Cdd:PLN02858  489 GCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVKDLG 568

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 694110399  248 LVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIFNGIT 294
Cdd:PLN02858  569 IVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLT 615
PLN02858 PLN02858
fructose-bisphosphate aldolase
 1-289 1.16e-51

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 182.36  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399    1 MTAHTNVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAGpSAVPFAAELDAVVLLVVNAAQVRGILF 80
Cdd:PLN02858    1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCD-SPAEAAKDAAALVVVLSHPDQVDDVFF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   81 GESGLAGHLKPGTAVMVSSTIASADAQAIAAALAE--YQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAV 158
Cdd:PLN02858   80 GDEGAAKGLQKGAVILIRSTILPLQLQKLEKKLTErkEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  159 AGKVYRIGSDIGLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSA 238
Cdd:PLN02858  160 CQKLYTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRF 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694110399  239 VDIFVKDLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKI 289
Cdd:PLN02858  240 LNVLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKV 290
garR PRK11559
tartronate semialdehyde reductase; Provisional
 10-290 4.08e-44

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 152.13  E-value: 4.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:PRK11559   8 IGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETA-STAKAVAEQCDVIITMLPNSPHVKEVALGENGIIEGA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  90 KPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGsDI 169
Cdd:PRK11559  87 KPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG-DI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVKDLGLV 249
Cdd:PRK11559 166 GAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLANA 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 694110399 250 NDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:PRK11559 246 LDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYY 286
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 6-166 4.79e-41

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: 139.91  E-value: 4.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399    6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGEsGL 85
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAA-ASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   86 AGHLKPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRI 165
Cdd:pfam03446  79 LPGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYI 158


                  .
gi 694110399  166 G 166
Cdd:pfam03446 159 G 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 10-290 4.15e-36

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: 131.07  E-value: 4.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:TIGR01692   2 IGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAA-ASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   90 KPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGsDI 169
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCG-DH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFE--NRMQHVLDG-----DYSPKSAVDIF 242
Cdd:TIGR01692 160 GAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPQapasnGYQGGFGTALM 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 694110399  243 VKDLGLVNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIKIF 290
Cdd:TIGR01692 240 LKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
10-287 2.91e-32

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 121.12  E-value: 2.91e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  10 IGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAGpSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:PRK15461   7 IGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAA-SPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCEGL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  90 KPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGSdI 169
Cdd:PRK15461  86 SRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG-P 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVT-HAAGNSWMFENRMQHVLDGDYSPKSAVDIFVKDLGL 248
Cdd:PRK15461 165 GMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSgTAAGKGHFTTTWPNKVLKGDLSPAFMIDLAHKDLGI 244

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 694110399 249 VNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVI 287
Cdd:PRK15461 245 ALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 170-288 1.68e-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: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRM-QHVLDGDYSPKSAVDIFVKDLGL 248
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFpQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 694110399  249 VNDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIK 288
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIR 120
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
10-288 2.02e-21

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 91.62  E-value: 2.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  10 IGLGSMGMGAARACLQAGLNTWGVDINPdNCRALLEAGAKGAgPSAVPFAAELDAVVLLVVNAAQVRGILFGESGLAGHL 89
Cdd:PRK15059   6 IGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVSV-ETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTKAS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  90 KPGTAVMVSSTIASADAQAIAAALAEYQLLMLDAPVSGGAVKAAAGDMTVMASGSDAVFARLAPVLDAVAGKVYRIGSDi 169
Cdd:PRK15059  84 LKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGGN- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399 170 GLGSTVKIIHQLLAGVHIAVAAEAMALAARAGIPLETMYDVVTHAAGNSWMFENRMQHVLDGDYSPKSAVDIFVKDLGLV 249
Cdd:PRK15059 163 GDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLNLA 242

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 694110399 250 NDTARALTFPLPLATTALNMFTSASNAGFGREDDSAVIK 288
Cdd:PRK15059 243 LQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQ 281
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
9-159 3.23e-06

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 47.82  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   9 VIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGAGpSAVPFAAELDA--VVLLVVNAAQVRGILFGEsgLA 86
Cdd:PRK09599   5 MIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGAD-SLEELVAKLPAprVVWLMVPAGEITDATIDE--LA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399  87 GHLKPGTAVM------VSSTIasadaqaiaaalAEYQLL------MLDAPVSGGaVKAAAGDMTVMASGSDAVFARLAPV 154
Cdd:PRK09599  82 PLLSPGDIVIdggnsyYKDDI------------RRAELLaekgihFVDVGTSGG-VWGLERGYCLMIGGDKEAVERLEPI 148


                 ....*
gi 694110399 155 LDAVA 159
Cdd:PRK09599 149 FKALA 153
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 6-100 3.32e-06

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: 47.43  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   6 NVCVIGLGSMGMGAARACLQAGLNT--WGVDINPDNCRALLEAGAKGAGPSAVPFAAELDAVVLLVVNAAQVRGILfgeS 83
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRAGLAHevVGVDRSPETLERALELGVIDRAATDLEEAVADADLVVLAVPVGATIEVL---A 79

                         90
                 ....*....|....*...
gi 694110399  84 GLAGHLKPGTAVM-VSST 100
Cdd:COG0287   80 ELAPHLKPGAIVTdVGSV 97
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 6-51 1.40e-03

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 38.67  E-value: 1.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 694110399    6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPD---NCRALLEAGAKGA 51
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEaleKALERIESSLERL 49
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 5-100 2.46e-03

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 39.12  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   5 TNVCVIGLGSMGMGAARACLQAGLNTWGVDINPDN--CRALLEAGAKGAGPSAVPFAAELDAVVLLVVNAAQVRGILfgE 82
Cdd:PRK06545   1 RTVLIVGLGLIGGSLALAIKAAGPDVFIIGYDPSAaqLARALGFGVIDELAADLQRAAAEADLIVLAVPVDATAALL--A 78

                         90
                 ....*....|....*....
gi 694110399  83 SGLAGHLKPGTAVM-VSST 100
Cdd:PRK06545  79 ELADLELKPGVIVTdVGSV 97
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 5-38 2.77e-03

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 38.55  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 694110399   5 TNVCVIGLGSMGMGAARACLQAGLNTWGVDINPD 38
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPE 36
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-51 3.99e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.07  E-value: 3.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 694110399   6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRALLEAGAKGA 51
Cdd:cd05188  137 TVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHV 182
WecC COG0677
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];
7-101 5.03e-03

UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440441 [Multi-domain]  Cd Length: 413  Bit Score: 38.12  E-value: 5.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   7 VCVIGLGSMGMGAARACLQAGLNTWGVDINPDNCRAL-------LEAGAK------GAG-------PSAVpfaAELDAVV 66
Cdd:COG0677    2 IAVIGLGYVGLPLAVAFAKAGFRVIGFDINPERVEELnagedpiLEPGDEllaeavAAGrlrattdPEAL---AEADVVI 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 694110399  67 LLV---------------VNAAQVrgilfgesgLAGHLKPGTAVMVSSTI 101
Cdd:COG0677   79 IAVptpldedkepdlsylESASET---------IAPHLKPGDLVVLESTV 119
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 6-92 9.44e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 37.37  E-value: 9.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694110399   6 NVCVIGLGSMGMGAARACLQAGLNTWGVDINPD---NCRALLEAGAK---GAGPSAVPFAAelDAVVL--------LVVN 71
Cdd:COG0771    6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPApelAAAELEAPGVEvvlGEHPEELLDGA--DLVVKspgippdhPLLK 83

                         90       100
                 ....*....|....*....|..
gi 694110399  72 AAQVRGI-LFGESGLAGHLKPG 92
Cdd:COG0771   84 AARAAGIpVIGEIELAYRLSPA 105
 
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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