|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
37-324 |
2.94e-169 |
|
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: 471.59 E-value: 2.94e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 37 FIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGILKKV 116
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 117 KKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCGQVG 196
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 197 TGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMEGVPSANNYQGGFGTTLMT 276
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41055658 277 KDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFLR 324
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
32-323 |
1.13e-111 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 325.53 E-value: 1.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 32 KTQVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNG 111
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 112 ILKKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVY 191
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 192 CGQVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPvpgvmegVPSANNYQGGFG 271
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41055658 272 TTLMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFL 323
Cdd:COG2084 234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
35-322 |
1.61e-66 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 211.06 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 35 VGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGILK 114
Cdd:PRK11559 5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 115 KVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCGQ 194
Cdd:PRK11559 85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 195 VGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEGvpsanNYQGGFGTTL 274
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIR--GGLAGSTVLDAKAPMVMDR-----NFKPGFRIDL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41055658 275 MTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQF 322
Cdd:PRK11559 238 HIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACY 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
34-193 |
2.80e-63 |
|
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: 197.69 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 34 QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPnGIL 113
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 114 KKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCG 193
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| PGDH_like_2 |
cd12172 |
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
27-123 |
5.36e-04 |
|
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.
Pssm-ID: 240649 [Multi-domain] Cd Length: 306 Bit Score: 41.32 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 27 RSMASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPEScKELQELGAQILdSPADVADKADRIITMLPSNP---NVV 103
Cdd:cd12172 138 TELYGKT-LGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDE-EFAKEHGVEFV-SLEELLKESDFISLHLPLTPetrHLI 214
|
90 100
....*....|....*....|
gi 41055658 104 DvytgpNGILKKVKKGSLLI 123
Cdd:cd12172 215 N-----AAELALMKPGAILI 229
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
37-324 |
2.94e-169 |
|
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: 471.59 E-value: 2.94e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 37 FIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGILKKV 116
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 117 KKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCGQVG 196
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 197 TGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMEGVPSANNYQGGFGTTLMT 276
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41055658 277 KDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFLR 324
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
32-323 |
1.13e-111 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 325.53 E-value: 1.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 32 KTQVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNG 111
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 112 ILKKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVY 191
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 192 CGQVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPvpgvmegVPSANNYQGGFG 271
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41055658 272 TTLMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFL 323
Cdd:COG2084 234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
35-322 |
1.61e-66 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 211.06 E-value: 1.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 35 VGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGILK 114
Cdd:PRK11559 5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 115 KVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCGQ 194
Cdd:PRK11559 85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 195 VGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEGvpsanNYQGGFGTTL 274
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIR--GGLAGSTVLDAKAPMVMDR-----NFKPGFRIDL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41055658 275 MTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQF 322
Cdd:PRK11559 238 HIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACY 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
34-193 |
2.80e-63 |
|
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: 197.69 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 34 QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPnGIL 113
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 114 KKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCG 193
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| tartro_sem_red |
TIGR01505 |
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
34-323 |
9.41e-59 |
|
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: 190.87 E-value: 9.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 34 QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGIL 113
Cdd:TIGR01505 1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 114 KKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCG 193
Cdd:TIGR01505 81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 194 QVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEgvpsaNNYQGGFGTT 273
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALR--GGLAGSTVLEVKGERVID-----RTFKPGFRID 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41055658 274 LMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFL 323
Cdd:TIGR01505 234 LHQKDLNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
32-328 |
1.00e-42 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 149.24 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 32 KTQVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNG 111
Cdd:PRK15461 1 MAAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 112 ILKKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVY 191
Cdd:PRK15461 81 VCEGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 192 CGQVGTGQAAKICNN-MLLAIGMIgTAETMNLGIRLGLDPKLLAKILN-MSSGRCWSSDTYnpvPG-VMEGVPSAnnyqg 268
Cdd:PRK15461 161 AGGPGMGIRVKLINNyMSIALNAL-SAEAAVLCEALGLSFDVALKVMSgTAAGKGHFTTTW---PNkVLKGDLSP----- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 269 GFGTTLMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFLREEEG 328
Cdd:PRK15461 232 AFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAG 291
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
34-323 |
4.95e-41 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 144.78 E-value: 4.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 34 QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPEScKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTGPNGIL 113
Cdd:PRK15059 2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 114 KKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMGANVVYCG 193
Cdd:PRK15059 81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 194 QVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLL----------AKILNMSSGRCWSSdTYNPvpgvmegvpsa 263
Cdd:PRK15059 161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVrqalmggfasSRILEVHGERMIKR-TFNP----------- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 264 nnyqgGFGTTLMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFL 323
Cdd:PRK15059 229 -----GFKIALHQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
29-319 |
2.93e-40 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 150.39 E-value: 2.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 29 MASKT--QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVY 106
Cdd:PLN02858 319 MQAKPvkRIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 107 TGPNGILKKVKKGSLLIDSSTIDPA-VSK-EMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSC 184
Cdd:PLN02858 399 FGDLGAVSALPAGASIVLSSTVSPGfVIQlERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 185 MGANV-VYCGQVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDtyNPVPGVMEgvpsa 263
Cdd:PLN02858 479 LSEKLyVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFE--NRVPHMLD----- 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41055658 264 NNYQGGFGTTLMTKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSV 319
Cdd:PLN02858 552 NDYTPYSALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAV 607
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
29-315 |
5.51e-37 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 141.14 E-value: 5.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 29 MASKTQVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADKADRIITMLPSNPNVVDVYTG 108
Cdd:PLN02858 1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 109 PNGILKKVKKGSLLIDSSTIDPA-VSK-EMAVAAEKLGAVFMGAPVSGGVGAATSGKLTFMVGGPEEEFNAAKELLSCMG 186
Cdd:PLN02858 81 DEGAAKGLQKGAVILIRSTILPLqLQKlEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 187 ANV-VYCGQVGTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSsdTYNPVPGVMEGVPSANN 265
Cdd:PLN02858 161 QKLyTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWI--FKNHVPLLLKDDYIEGR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41055658 266 YQGGFgttlmTKDLGLAQNSATNTKTPVLLGSVAHQiyRMMCGRGYANKD 315
Cdd:PLN02858 239 FLNVL-----VQNLGIVLDMAKSLPFPLPLLAVAHQ--QLISGSSSMQGD 281
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
196-323 |
1.80e-31 |
|
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: 114.54 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 196 GTGQAAKICNNMLLAIGMIGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYnpvpgvMEGVPSANNYQGGFGTTLM 275
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENK------FPQRVLSRDFDPGFALDLM 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 41055658 276 TKDLGLAQNSATNTKTPVLLGSVAHQIYRMMCGRGYANKDFSSVFQFL 323
Cdd:pfam14833 75 LKDLGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
34-212 |
1.75e-19 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 87.11 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 34 QVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSPADVADK--ADRII-TMLPSNPNVVDVYtgpN 110
Cdd:PRK09599 2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKlpAPRVVwLMVPAGEITDATI---D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 111 GILKKVKKGSLLID---SSTIDpavSKEMAVAAEKLGAVFMGAPVSGGVGAATSGkLTFMVGGPEEEFNAAKEL---LSC 184
Cdd:PRK09599 79 ELAPLLSPGDIVIDggnSYYKD---DIRRAELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIfkaLAP 154
|
170 180 190
....*....|....*....|....*....|....
gi 41055658 185 MGAN-VVYCGQVGTGQAAKICNN-----MLLAIG 212
Cdd:PRK09599 155 RAEDgYLHAGPVGAGHFVKMVHNgieygMMQAYA 188
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
31-93 |
1.56e-09 |
|
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: 57.77 E-value: 1.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055658 31 SKTQVGFIGLGNMGNPMAKNLIKHGYP---VIATDVFPESCKELQE-LGAQILDSPADVADKADRII 93
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVV 67
|
|
| PTZ00142 |
PTZ00142 |
6-phosphogluconate dehydrogenase; Provisional |
32-206 |
5.08e-09 |
|
6-phosphogluconate dehydrogenase; Provisional
Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 57.11 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 32 KTQVGFIGLGNMGNPMAKNLIKHGYPVIA-------TDVFPESCKE--LQELGAQILDSPADVADKADRIITMLPSNPnV 102
Cdd:PTZ00142 1 MSDIGLIGLAVMGQNLALNIASRGFKISVynrtyekTEEFVKKAKEgnTRVKGYHTLEELVNSLKKPRKVILLIKAGE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 103 VDVYTgpNGILKKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKlTFMVGGPEEEFNAAKELL 182
Cdd:PTZ00142 80 VDETI--DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDIL 156
|
170 180 190
....*....|....*....|....*....|
gi 41055658 183 SCMGANV------VYCGQVGTGQAAKICNN 206
Cdd:PTZ00142 157 EKCSAKVgdspcvTYVGPGSSGHYVKMVHN 186
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
31-93 |
4.91e-08 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 53.23 E-value: 4.91e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055658 31 SKTQVGFIGLGNMGNPMAKNLIKHGYP---VIATDVFPESCKEL-QELGAQILDSPADVADKADRII 93
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVV 67
|
|
| PLN02350 |
PLN02350 |
phosphogluconate dehydrogenase (decarboxylating) |
28-206 |
1.36e-06 |
|
phosphogluconate dehydrogenase (decarboxylating)
Pssm-ID: 215200 [Multi-domain] Cd Length: 493 Bit Score: 49.71 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 28 SMASKTQVGFIGLGNMGNPMAKNLIKHGYPVI----ATDVFPESCKELQELGAQILDSPADVAD-----KADRIITMLPS 98
Cdd:PLN02350 2 ASAALSRIGLAGLAVMGQNLALNIAEKGFPISvynrTTSKVDETVERAKKEGNLPLYGFKDPEDfvlsiQKPRSVIILVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 99 NPNVVDVYTgpNGILKKVKKGSLLIDSSTIDPAVSKEMAVAAEKLGAVFMGAPVSGGVGAATSGKlTFMVGGPEEEFNAA 178
Cdd:PLN02350 82 AGAPVDQTI--KALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNI 158
|
170 180 190
....*....|....*....|....*....|....
gi 41055658 179 KELLSCM------GANVVYCGQVGTGQAAKICNN 206
Cdd:PLN02350 159 EDILEKVaaqvddGPCVTYIGPGGAGNFVKMVHN 192
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
35-103 |
1.06e-04 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 43.02 E-value: 1.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055658 35 VGFIGLGNMGNPMAKNLIKHGYPV-----IATDVFPESCKELQELGAQILDSPADVADKADRIItmLPSNPNVV 103
Cdd:PLN02688 3 VGFIGAGKMAEAIARGLVASGVVPpsrisTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVII--LAVKPQVV 74
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
39-140 |
2.84e-04 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 42.28 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 39 GLGNMGNPMAKNLIKHGYPVIATDVFPESCKEL-QELGAQILDSPADVADKADRIITMLPSN--PNVVDvYTGPngilkK 115
Cdd:PRK08655 8 GTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVaKELGVEYANDNIDAAKDADIVIISVPINvtEDVIK-EVAP-----H 81
|
90 100
....*....|....*....|....*
gi 41055658 116 VKKGSLLIDSSTIdpavsKEMAVAA 140
Cdd:PRK08655 82 VKEGSLLMDVTSV-----KERPVEA 101
|
|
| PGDH_like_2 |
cd12172 |
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
27-123 |
5.36e-04 |
|
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.
Pssm-ID: 240649 [Multi-domain] Cd Length: 306 Bit Score: 41.32 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 27 RSMASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPEScKELQELGAQILdSPADVADKADRIITMLPSNP---NVV 103
Cdd:cd12172 138 TELYGKT-LGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDE-EFAKEHGVEFV-SLEELLKESDFISLHLPLTPetrHLI 214
|
90 100
....*....|....*....|
gi 41055658 104 DvytgpNGILKKVKKGSLLI 123
Cdd:cd12172 215 N-----AAELALMKPGAILI 229
|
|
| PTDH |
cd12157 |
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ... |
21-147 |
7.47e-04 |
|
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.
Pssm-ID: 240634 [Multi-domain] Cd Length: 318 Bit Score: 40.73 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 21 AVQVSIRSMASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQILDSpADVADKADRIITMLPSNP 100
Cdd:cd12157 134 RPKFYGTGLDGKT-VGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVEL-DELLESSDFLVLALPLTP 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 41055658 101 nvvDVYTGPNG-ILKKVKKGSLLIDSSTidPAVSKEMAVA----AEKLGA----VF 147
Cdd:cd12157 212 ---DTLHLINAeALAKMKPGALLVNPCR--GSVVDEAAVAealkSGHLGGyaadVF 262
|
|
| 2-Hacid_dh_14 |
cd12179 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; ... |
29-85 |
1.80e-03 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases, NAD-binding and catalytic domains; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240656 [Multi-domain] Cd Length: 306 Bit Score: 39.58 E-value: 1.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 41055658 29 MASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPE-SCKELQELGAQILDSPADV 85
Cdd:cd12179 136 LMGKT-VGIIGYGNMGKAFAKRLSGFGCKVIAYDKYKNfGDAYAEQVSLETLFKEADI 192
|
|
| CtBP_dh |
cd05299 |
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ... |
26-126 |
1.87e-03 |
|
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.
Pssm-ID: 240624 [Multi-domain] Cd Length: 312 Bit Score: 39.42 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 26 IRSMASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPESCKElqELGAQILDSPADVADKADRIITMLPSNP---NV 102
Cdd:cd05299 137 IRRLRGLT-LGLVGFGRIGRAVAKRAKAFGFRVIAYDPYVPDGVA--ALGGVRVVSLDELLARSDVVSLHCPLTPetrHL 213
|
90 100
....*....|....*....|....
gi 41055658 103 VDVYTgpngiLKKVKKGSLLIDSS 126
Cdd:cd05299 214 IDAEA-----LALMKPGAFLVNTA 232
|
|
| LDH_like |
cd01619 |
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ... |
1-126 |
3.38e-03 |
|
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.
Pssm-ID: 240620 [Multi-domain] Cd Length: 323 Bit Score: 38.82 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 1 MAALLRVSRCLVVKCNNHVNAVQVSI-RSMASKTqVGFIGLGNMGNPMAKNLIKHGYPVIATDVFPEscKELQELGAQiL 79
Cdd:cd01619 112 ILALLRNRKYIDERDKNQDLQDAGVIgRELEDQT-VGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRN--PELEDKGVK-Y 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 41055658 80 DSPADVADKADrIITM-LPSNPNVVDVYTGPNgiLKKVKKGSLLIDSS 126
Cdd:cd01619 188 VSLEELFKNSD-IISLhVPLTPENHHMINEEA--FKLMKKGVIIINTA 232
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
38-98 |
4.59e-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: 38.12 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055658 38 IGLGNMGNPMAKNLIKHGYPVIATDVFPESCKELQELGAQIL-DSPADV-------ADKADRIITMLPS 98
Cdd:COG0569 101 IGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIvGDATDEevleeagIEDADAVIAATGD 169
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
36-124 |
4.70e-03 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 35.67 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055658 36 GFIGLGNMGNPMAKNLIKHGYP--VIATDVFPESCKEL-QELGAQIL-DSPADVADKADRIITMLPSnPNVVDVytgpNG 111
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELaEEYGVGATaVDNEEAAEEADVVFLAVKP-EDAPDV----LS 75
|
90
....*....|...
gi 41055658 112 ILKKVKKGSLLID 124
Cdd:pfam03807 76 ELSDLLKGKIVIS 88
|
|
| |
