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Conserved domains on  [gi|446641547|ref|WP_000718893|]
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MULTISPECIES: sulfolactaldehyde 3-reductase [Enterobacteriaceae]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11487806)

NAD(P)-dependent oxidoreductase such as sulfolactaldehyde 3-reductase, which reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-296 0e+00

sulfolactaldehyde 3-reductase;


:

Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 560.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:PRK15461   1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:PRK15461  81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHK 240
Cdd:PRK15461 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNKVLKGDLSPAFMIDLAHK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446641547 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGMTAKV 296
Cdd:PRK15461 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGLTAKV 296
 
Name Accession Description Interval E-value
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-296 0e+00

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 560.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:PRK15461   1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:PRK15461  81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHK 240
Cdd:PRK15461 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNKVLKGDLSPAFMIDLAHK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446641547 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGMTAKV 296
Cdd:PRK15461 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGLTAKV 296
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-286 1.19e-100

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 296.26  E-value: 1.19e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPnKVLSGDLSPAFMIDLAHK 240
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-RMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446641547 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQV 286
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-287 8.14e-61

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: 195.02  E-value: 8.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    6 FIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCEGL 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   86 STDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGGPG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  166 MGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTT--SWPNKV----LSGDLSPAFMIDLAH 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTynPVPGVMpqapASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 446641547  240 KDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-162 3.62e-54

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: 173.42  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGEnGVCE 83
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446641547   84 GLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAG 162
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
 
Name Accession Description Interval E-value
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-296 0e+00

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 560.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:PRK15461   1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:PRK15461  81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHK 240
Cdd:PRK15461 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNKVLKGDLSPAFMIDLAHK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446641547 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGMTAKV 296
Cdd:PRK15461 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGLTAKV 296
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-286 1.19e-100

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 296.26  E-value: 1.19e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:COG2084   81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPnKVLSGDLSPAFMIDLAHK 240
Cdd:COG2084  161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-RMLAGDFDPGFALDLMLK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446641547 241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQV 286
Cdd:COG2084  240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-282 5.01e-66

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 208.37  E-value: 5.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENG 80
Cdd:PRK11559   2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELIN 160
Cdd:PRK11559  82 IIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 161 AGGPGMGIRVKLINNYMsIALN-ALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPnKVLSGDLSPAFMIDLAH 239
Cdd:PRK11559 162 TGDIGAGNVTKLANQVI-VALNiAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHI 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446641547 240 KDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAI 282
Cdd:PRK11559 240 KDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSAL 282
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-287 8.14e-61

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: 195.02  E-value: 8.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    6 FIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCEGL 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   86 STDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGGPG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  166 MGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTT--SWPNKV----LSGDLSPAFMIDLAH 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTynPVPGVMpqapASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 446641547  240 KDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 4-291 4.58e-57

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: 185.48  E-value: 4.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCE 83
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   84 GLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGG 163
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  164 PGMGIRVKLINNYMsIALN-ALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNkVLSGDLSPAFMIDLAHKDL 242
Cdd:TIGR01505 162 NGDGQTCKVANQII-VALNiEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGER-VIDRTFKPGFRIDLHQKDL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 446641547  243 GIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAG 291
Cdd:TIGR01505 240 NLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLAN 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 4-162 3.62e-54

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: 173.42  E-value: 3.62e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGEnGVCE 83
Cdd:pfam03446   2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446641547   84 GLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAG 162
Cdd:pfam03446  81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PLN02858 PLN02858
fructose-bisphosphate aldolase
 4-284 1.28e-39

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 147.69  E-value: 1.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCE 83
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVS 406

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   84 GLSTDALVIDMSTIHPLQTDKLIADMQA--KGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSEL-IN 160
Cdd:PLN02858  407 ALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyVI 486

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNkVLSGDLSPAFMIDLAHK 240
Cdd:PLN02858  487 KGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPH-MLDNDYTPYSALDIFVK 565

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 446641547  241 DLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILE 284
Cdd:PLN02858  566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVK 609
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-292 2.99e-37

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 140.76  E-value: 2.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547    2 AAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGV 81
Cdd:PLN02858    5 GVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   82 CEGLSTDALVIDMSTIHPLQTDKL---IADMQAKGFsMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSEL 158
Cdd:PLN02858   85 AKGLQKGAVILIRSTILPLQLQKLekkLTERKEQIF-LVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  159 -INAGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPnKVLSGDLSPAFMIDL 237
Cdd:PLN02858  164 yTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVP-LLLKDDYIEGRFLNV 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446641547  238 AHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGM 292
Cdd:PLN02858  243 LVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGV 297
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
4-290 5.42e-35

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 128.22  E-value: 5.42e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAvRHLVDKGATPAANPAQAAKDAEFIITMLPNGDLVRNVLFGENGVCE 83
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  84 GLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTLLLLAGGTAEQVERATPILMAMGSELINAGG 163
Cdd:PRK15059  82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 164 PGMGIRVKLINNYMsIALN--ALSAEAAVLCEALNLPFDVAVKVMSGTAAGKghFTTSWPNKVLSGDLSPAFMIDLAHKD 241
Cdd:PRK15059 162 NGDGQTCKVANQII-VALNieAVSEALLFASKAGADPVRVRQALMGGFASSR--ILEVHGERMIKRTFNPGFKIALHQKD 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446641547 242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSA 290
Cdd:PRK15059 239 LNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMA 287
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 165-283 2.61e-22

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: 89.51  E-value: 2.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  165 GMGIRVKLINNYMSIALNALSAEAAVLCEALNLPFDVAVKVMSGTAAGKGHFTTSWPNKVLSGDLSPAFMIDLAHKDLGI 244
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 446641547  245 ALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAIL 283
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAII 119
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
4-175 6.22e-18

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 82.10  E-value: 6.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPAQ--AAKDAEFII-TMLPNGDLVRNVLfgeNG 80
Cdd:PRK09599   3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEElvAKLPAPRVVwLMVPAGEITDATI---DE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  81 VCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVG------RTSANaitgtllLLAGGTAEQVERATPIL--M 152
Cdd:PRK09599  80 LAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSggvwglERGYC-------LMIGGDKEAVERLEPIFkaL 152

                        170       180
                 ....*....|....*....|....*
gi 446641547 153 AMGSE--LINAGGPGMGIRVKLINN 175
Cdd:PRK09599 153 APRAEdgYLHAGPVGAGHFVKMVHN 177
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 4-62 7.12e-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: 49.29  E-value: 7.12e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446641547   4 IAFIGLGQMGSPMASNLLQQG---HQLRVFDVNAEAVRHLVDK-GATPAANPAQAAKDAEFII 62
Cdd:COG0345    5 IGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVV 67
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-62 2.61e-05

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 44.75  E-value: 2.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQG---HQLRVFDVNAEAVRHLVDK-GATPAANPAQAAKDAEFII 62
Cdd:PRK11880   2 MKKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-210 9.04e-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: 40.18  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLR-VFDVNAEAVRHLVDK-GATPAANPAQAAKDAEFIITMLPNGDLVrnvlfge 78
Cdd:COG5495    3 RMKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALlGAVPALDLEELAAEADLVLLAVPDDAIA------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  79 nGVCEGLST------DALVIDMS-------------------TIHPLQTdkliadmqakgFSmmdvpVGRTSANAITGTL 133
Cdd:COG5495   76 -EVAAGLAAagalrpGQLVVHTSgalgsdvlapaaragaltgSFHPLQT-----------FS-----GPREDLERLAGIP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547 134 LLLAGGtAEQVERATPILMAMGSE--LINAGGpgmgiRVKL------INNYmsiaLNALSAEAAVLCEALNL--PFDVAV 203
Cdd:COG5495  139 FAIEGD-EEALPVLEALAEALGGEpfVIDSEQ-----RPLYhaaavfASNF----LVTLVALAAELLEAAGLedAFDALL 208


                 ....*..
gi 446641547 204 KVMSGTA 210
Cdd:COG5495  209 PLIRETL 215
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 1-191 9.82e-04

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 40.54  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   1 MAAIAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGATPAANPA---------QAAKDAEFIITMLPNGDLV 71
Cdd:PTZ00142   1 MSDIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNTRVKgyhtleelvNSLKKPRKVILLIKAGEAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547  72 RNVLfgeNGVCEGLSTDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSANAITGTlLLLAGGTAEQVERATPIL 151
Cdd:PTZ00142  81 DETI---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDIL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446641547 152 MAMGSELINA------GGPGMGIRVKLINNYMSIALNALSAEAAVL 191
Cdd:PTZ00142 157 EKCSAKVGDSpcvtyvGPGSSGHYVKMVHNGIEYGDMQLISESYKL 202
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
4-71 1.15e-03

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 39.38  E-value: 1.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDK---GATPAANpAQAAKDAEFIITMLPNGDLV 71
Cdd:COG2085    1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAElgpGARAGTN-AEAAAAADVVVLAVPYEAVP 70
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-62 2.31e-03

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: 38.95  E-value: 2.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRV--FDVNAEAVRHLVDKGA--TPAANPAQAAKDAEFII 62
Cdd:COG0287    4 IAIIGLGLIGGSLALALKRAGLAHEVvgVDRSPETLERALELGVidRAATDLEEAVADADLVV 66
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 4-62 6.69e-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: 37.40  E-value: 6.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAV-----------RHLVDKGATPAANPAQ------------AAKDAEF 60
Cdd:COG1250    5 VAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALerarariakllDKLVKKGKLTEEEADAalaritpttdlaALADADL 84


                 ..
gi 446641547  61 II 62
Cdd:COG1250   85 VI 86
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 4-45 6.99e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 37.35  E-value: 6.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446641547   4 IAFIGLGQMGSPMASNLLQQGHQLRVFDVNAEAVRHLVDKGA 45
Cdd:COG0569   98 VIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDV 139
 
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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