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Conserved domains on  [gi|1301388631|gb|PKB58044|]
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MAG: 3-hydroxyisobutyrate dehydrogenase [SAR202 cluster bacterium Casp-Chloro-G3]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-287 1.30e-105

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


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.74  E-value: 1.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:COG2084    81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILhEGLVRTMFRGTFEPaSFALNLA 240
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVL-SGGAAGSWVL-ENRGPRMLAGDFDP-GFALDLM 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1301388631 241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLL 287
Cdd:COG2084   238 LKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKL 284
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-287 1.30e-105

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.74  E-value: 1.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:COG2084    81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILhEGLVRTMFRGTFEPaSFALNLA 240
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVL-SGGAAGSWVL-ENRGPRMLAGDFDP-GFALDLM 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1301388631 241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLL 287
Cdd:COG2084   238 LKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKL 284
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-297 1.97e-78

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 241.11  E-value: 1.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:PRK11559    2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:PRK11559   82 IIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRRGSLGRMrILHEGLVRTMFRgTFEPAsFALNLA 240
Cdd:PRK11559  162 TGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGST-VLDAKAPMVMDR-NFKPG-FRIDLH 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1301388631 241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAGVEIR 297
Cdd:PRK11559  239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVT 295
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 4-296 9.33e-64

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: 203.20  E-value: 9.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   4 VGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEGVLE 83
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  84 GIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAGA 163
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 164 IGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILHEGLVRTMFRgTFEPAsFALNLAYKD 243
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQAL-RGGLAGSTVLEVKGERVIDR-TFKPG-FRIDLHQKD 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1301388631 244 ISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAGVEI 296
Cdd:TIGR01505 239 LNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-162 2.78e-56

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: 179.59  E-value: 2.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   3 TVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGdEGVL 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  83 EGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAG 162
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-287 1.30e-105

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


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 309.74  E-value: 1.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:COG2084     1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:COG2084    81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILhEGLVRTMFRGTFEPaSFALNLA 240
Cdd:COG2084   161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVL-SGGAAGSWVL-ENRGPRMLAGDFDP-GFALDLM 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1301388631 241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLL 287
Cdd:COG2084   238 LKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKL 284
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-297 1.97e-78

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 241.11  E-value: 1.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:PRK11559    2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:PRK11559   82 IIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRRGSLGRMrILHEGLVRTMFRgTFEPAsFALNLA 240
Cdd:PRK11559  162 TGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGST-VLDAKAPMVMDR-NFKPG-FRIDLH 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1301388631 241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAGVEIR 297
Cdd:PRK11559  239 IKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVT 295
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 4-296 9.33e-64

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: 203.20  E-value: 9.33e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   4 VGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEGVLE 83
Cdd:TIGR01505   2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  84 GIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAGA 163
Cdd:TIGR01505  82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 164 IGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILHEGLVRTMFRgTFEPAsFALNLAYKD 243
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQAL-RGGLAGSTVLEVKGERVIDR-TFKPG-FRIDLHQKD 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1301388631 244 ISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAGVEI 296
Cdd:TIGR01505 239 LNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 6-288 1.12e-59

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: 192.71  E-value: 1.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   6 FIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEGVLEGI 85
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  86 RPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAGAIG 165
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 166 AGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRRGSLGRMRILHEGLVRTMFRGTfePAS------FALNL 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQA--PASngyqggFGTAL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1301388631 240 AYKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRD-SSVTVLLQ 288
Cdd:TIGR01692 239 MLKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDfSSVIQLLR 288
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 3-162 2.78e-56

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: 179.59  E-value: 2.78e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   3 TVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGdEGVL 82
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  83 EGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAG 162
Cdd:pfam03446  80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
1-278 6.82e-47

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 160.02  E-value: 6.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:PRK15461    1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 VLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFY 160
Cdd:PRK15461   81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 161 AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMR--RGSLGRMRILHEGLVrtmFRGTFEPAsFALN 238
Cdd:PRK15461  161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSgtAAGKGHFTTTWPNKV---LKGDLSPA-FMID 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1301388631 239 LAYKDISLATELAKEYNVPMPMTTLAEQITLQA--MNRGWQD 278
Cdd:PRK15461  237 LAHKDLGIALDVANQLHVPMPLGAASREVYSQAraAGRGRQD 278
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
4-288 2.05e-46

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 158.65  E-value: 2.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   4 VGFIGLGNMGGGMSANIQRAGYPMVVFDLrEEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEGVLE 83
Cdd:PRK15059    3 LGFIGLGIMGTPMAINLARAGHQLHVTTI-GPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  84 GIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYAGA 163
Cdd:PRK15059   82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 164 IGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMrRGSLGRMRILHEGLVRtMFRGTFEPAsFALNLAYKD 243
Cdd:PRK15059  162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQAL-MGGFASSRILEVHGER-MIKRTFNPG-FKIALHQKD 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1301388631 244 ISLATELAKEYNVPMPMT-TLAEQITLQAMNRGWQDRDSSVTVLLQ 288
Cdd:PRK15059  239 LNLALQSAKALALNLPNTaTCQELFNTCAANGGSQLDHSALVQALE 284
PLN02858 PLN02858
fructose-bisphosphate aldolase
 4-316 9.22e-41

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 151.54  E-value: 9.22e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631    4 VGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEGVLE 83
Cdd:PLN02858     7 VGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAAK 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   84 GIRPGSIYIDLSSSRPTLIRELEPKF--RQKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFGDKVFYA 161
Cdd:PLN02858    87 GLQKGAVILIRSTILPLQLQKLEKKLteRKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYTF 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  162 -GAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRRGSlGRMRILHEgLVRTMFRGTFEPASFaLNLA 240
Cdd:PLN02858   167 eGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAA-GSSWIFKN-HVPLLLKDDYIEGRF-LNVL 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  241 YKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAGVEIRAPHI----DPVKSGKFITTHPDA 316
Cdd:PLN02858   244 VQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNILEAANrelyKPEDLAKQITMQAKP 323
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-299 7.05e-38

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 143.07  E-value: 7.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631    2 ETVGFIGLGNMGGGMSANIQRAGYPMVVFDlreeVTKPLL----EGGARLANSPAQVAELSDVTFSSLPGPKEVESVVLG 77
Cdd:PLN02858   325 KRIGFIGLGAMGFGMASHLLKSNFSVCGYD----VYKPTLvrfeNAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFG 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   78 DEGVLEGIRPGSIYIDLSSSRPTLIRELEPKFR--QKGCYVLDAPVSGGKSGADSGNLAVMVGGDREIFEKVKPILDAFG 155
Cdd:PLN02858   401 DLGAVSALPAGASIVLSSTVSPGFVIQLERRLEneGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALS 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  156 DKVFY-AGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRRGslGRMRILHEGLVRTMFRGTFEPAS 234
Cdd:PLN02858   481 EKLYViKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNA--GGTSWMFENRVPHMLDNDYTPYS 558

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1301388631  235 fALNLAYKDISLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSSVTVLLQEEQAG--VEIRAP 299
Cdd:PLN02858   559 -ALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGvkVEGRLP 624
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-210 9.01e-31

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


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 117.50  E-value: 9.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 MEtVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQ-VAELSD--VTFSSLPGPKEVESVVlg 77
Cdd:COG1023     1 MQ-IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEElVAKLPAprVVWLMVPAGEITDQVI-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  78 dEGVLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGnLAVMVGGDREIFEKVKPILDA---- 153
Cdd:COG1023    78 -EELAPLLEPGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFKAlapg 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1301388631 154 FGDKVFYAGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVE--PEAVWECMRRGS 210
Cdd:COG1023   156 AENGYLHCGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASEFDldLAEVAEVWRRGS 214
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-210 2.00e-30

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 116.39  E-value: 2.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 MEtVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLANSPAQ-VAELSD--VTFSSLPGPKEVESVVlg 77
Cdd:PRK09599    1 MQ-LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEElVAKLPAprVVWLMVPAGEITDATI-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  78 dEGVLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGGKSGADSGnLAVMVGGDREIFEKVKPILDA---F 154
Cdd:PRK09599   78 -DELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKAlapR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1301388631 155 GDKVF-YAGAIGAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVE--PEAVWECMRRGS 210
Cdd:PRK09599  156 AEDGYlHAGPVGAGHFVKMVHNGIEYGMMQAYAEGFELLEASRFDldLAAVAEVWRRGS 214
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 165-282 4.28e-26

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: 99.91  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631 165 GAGSICKLVHNMIGHSVRQAIAEGLTLGVKAGVEPEAVWECMRrGSLGRMRILHEGLVRTMFRGTFEPAsFALNLAYKDI 244
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLN-GGSGRSNALENKFPQRVLSRDFDPG-FALDLMLKDL 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1301388631 245 SLATELAKEYNVPMPMTTLAEQITLQAMNRGWQDRDSS 282
Cdd:pfam14833  79 GLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHS 116
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 4-187 3.04e-12

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 66.64  E-value: 3.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   4 VGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLAN-SPAQ-VAELSDvtfsSLPGP----------KEV 71
Cdd:COG0362     5 IGVIGLAVMGRNLALNIADHGFSVAVYNRTAEKTDAFLAEHGKGKNiVGTYsLEEFVA----SLERPrkillmvkagKPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  72 ESVVlgdEGVLEGIRPGSIYIDLSSS--RPTLIRELEpkFRQKGCYVLDAPVSGGKSGADSGNlAVMVGGDREIFEKVKP 149
Cdd:COG0362    81 DAVI---EQLLPLLEPGDIIIDGGNShfTDTIRREKE--LAEKGIHFIGMGVSGGEEGALHGP-SIMPGGSKEAYELVKP 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1301388631 150 ILDAFGDKV------FYAGAIGAGSICKLVHNMIGHSVRQAIAE 187
Cdd:COG0362   155 ILEAIAAKVdgepcvTYIGPDGAGHFVKMVHNGIEYADMQLIAE 198
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 1-187 4.30e-12

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 66.35  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLEGgARLANSPAQVAELSDVTFSSLPGPKEVESVVLGDEG 80
Cdd:PTZ00142    1 MSDIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKK-AKEGNTRVKGYHTLEELVNSLKKPRKVILLIKAGEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  81 V---LEGIRP----GSIYID------LSSSRPTLirelepKFRQKGCYVLDAPVSGGKSGADSGNlAVMVGGDREIFEKV 147
Cdd:PTZ00142   80 VdetIDNLLPllekGDIIIDggnewyLNTERRIK------RCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHV 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1301388631 148 KPILDAFGDKV------FYAGAIGAGSICKLVHNMIGHSVRQAIAE 187
Cdd:PTZ00142  153 KDILEKCSAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISE 198
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 4-187 7.19e-10

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 59.73  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   4 VGFIGLGNMGGGMSANIQRAGYPMVVFD-----LREEVTKPLLEGGARLA--NSPAQVAelsdvtfSSLPGPKEVESVVL 76
Cdd:PLN02350    9 IGLAGLAVMGQNLALNIAEKGFPISVYNrttskVDETVERAKKEGNLPLYgfKDPEDFV-------LSIQKPRSVIILVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  77 GDEGVLEGIR-------PGSIYIDLSSS--RPTLIRELEpkFRQKGCYVLDAPVSGGKSGADSGNlAVMVGGDREIFEKV 147
Cdd:PLN02350   82 AGAPVDQTIKalseymePGDCIIDGGNEwyENTERRIKE--AAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1301388631 148 KPILDAF------GDKVFYAGAIGAGSICKLVHNMIGHSVRQAIAE 187
Cdd:PLN02350  159 EDILEKVaaqvddGPCVTYIGPGGAGNFVKMVHNGIEYGDMQLISE 204
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
12-187 1.00e-07

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 52.82  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  12 MGGGMSANIQRAGYPMVVFDLREEVTKPLLEGGARLAN-SPAqvAELSDvtF-SSLPGP-KEVESVVLGD--EGVLEGIR 86
Cdd:PRK09287    1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEEGKGKKiVPA--YTLEE--FvASLEKPrKILLMVKAGApvDAVIEQLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  87 P----GSIYIDLSSS--RPTLIRELEpkFRQKGCYVLDAPVSGGKSGADSGNlAVMVGGDREIFEKVKPILDAFGDKVF- 159
Cdd:PRK09287   77 PllekGDIIIDGGNSnyKDTIRREKE--LAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEKIAAKVEd 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1301388631 160 ------YAGAIGAGSICKLVHNMIGHSVRQAIAE 187
Cdd:PRK09287  154 gepcvtYIGPDGAGHYVKMVHNGIEYGDMQLIAE 187
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-62 1.26e-04

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 42.83  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYP---MVVFDLREEVTKPLLEG-GARLANSPAQVAELSDVTF 62
Cdd:PRK11880    2 MKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-163 2.50e-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: 42.04  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPM--VVFDLREEVTKPLLEGGA--RLANSPAQVAELSDVTFSSLPgPKEVESVVl 76
Cdd:COG0287     1 FMRIAIIGLGLIGGSLALALKRAGLAHevVGVDRSPETLERALELGVidRAATDLEEAVADADLVVLAVP-VGATIEVL- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631  77 gdEGVLEGIRPGSIYIDLSSSRPTLIRELEPKFRQKGCYVLDAPVSGG-KSGADSGNL-----AVMV-----GGDREIFE 145
Cdd:COG0287    79 --AELAPHLKPGAIVTDVGSVKGAVVEAAEALLPDGVRFVGGHPMAGTeKSGPEAADAdlfegAPYIltpteGTDPEALE 156

                         170
                  ....*....|....*...
gi 1301388631 146 KVKPILDAFGDKVFYAGA 163
Cdd:COG0287   157 RVEELWEALGARVVEMDP 174
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 3-87 5.75e-04

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: 40.82  E-value: 5.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   3 TVGFIGLGNMGGGMSANIQRAGYP---MVVFDLREEVTKPLLE-GGARLANSPAQVAELSDVTFSSLPgPKEVESvvlgd 78
Cdd:COG0345     4 KIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVVLAVK-PQDLAE----- 77


                  ....*....
gi 1301388631  79 egVLEGIRP 87
Cdd:COG0345    78 --VLEELAP 84
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
5-95 2.44e-03

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 36.44  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301388631   5 GFIGLGNMGGGMSANIQRAGYPMVVFDLR---EEVTKPLLEGGARL-ANSPAQVAELSDVTFSSLPgPKEVESVVlgdeG 80
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGPHEVVVANSrnpEKAEELAEEYGVGAtAVDNEEAAEEADVVFLAVK-PEDAPDVL----S 75

                          90
                  ....*....|....*
gi 1301388631  81 VLEGIRPGSIYIDLS 95
Cdd:pfam03807  76 ELSDLLKGKIVISIA 90
PRK06035 PRK06035
3-hydroxyacyl-CoA dehydrogenase; Validated
 1-42 8.44e-03

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 180361 [Multi-domain]  Cd Length: 291  Bit Score: 37.16  E-value: 8.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1301388631   1 METVGFIGLGNMGGGMSANIQRAGYPMVVFDLREEVTKPLLE 42
Cdd:PRK06035    3 IKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILKNAME 44
 
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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