|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
37-324 |
1.30e-166 |
|
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: 465.04 E-value: 1.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 37 FIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILRKV 116
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 117 KKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQVG 196
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 197 SGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMEGVPSANNYQGGFITTLMA 276
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50417829 277 KDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFLR 324
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
32-323 |
4.85e-112 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 326.69 E-value: 4.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 32 KTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNS 111
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 112 ILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVY 191
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 192 CGQVGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPvpgvmegVPSANNYQGGFI 271
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 50417829 272 TTLMAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFL 323
Cdd:COG2084 234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
35-322 |
1.74e-68 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 216.07 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILR 114
Cdd:PRK11559 5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQ 194
Cdd:PRK11559 85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 195 VGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEGvpsanNYQGGFITTL 274
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIR--GGLAGSTVLDAKAPMVMDR-----NFKPGFRIDL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50417829 275 MAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQF 322
Cdd:PRK11559 238 HIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACY 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
35-193 |
2.72e-61 |
|
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: 192.68 E-value: 2.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSnSILR 114
Cdd:pfam03446 2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCG 193
Cdd:pfam03446 81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| LDH_like |
cd01619 |
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ... |
1-126 |
1.67e-04 |
|
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: 42.67 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 1 MAALFRGYRNFYKRSNKHVELIL-VSCRSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEscKELQDSGAQiL 79
Cdd:cd01619 112 ILALLRNRKYIDERDKNQDLQDAgVIGRELEDQT-VGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRN--PELEDKGVK-Y 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 50417829 80 DSPAEVAEKADrIITM-LPSSPNVIEVYTGSNsiLRKVKKGTLLIDSS 126
Cdd:cd01619 188 VSLEELFKNSD-IISLhVPLTPENHHMINEEA--FKLMKKGVIIINTA 232
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
37-324 |
1.30e-166 |
|
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: 465.04 E-value: 1.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 37 FIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILRKV 116
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 117 KKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQVG 196
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 197 SGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMEGVPSANNYQGGFITTLMA 276
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50417829 277 KDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFLR 324
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
32-323 |
4.85e-112 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 326.69 E-value: 4.85e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 32 KTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNS 111
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 112 ILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVY 191
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 192 CGQVGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPvpgvmegVPSANNYQGGFI 271
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 50417829 272 TTLMAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFL 323
Cdd:COG2084 234 LDLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
35-322 |
1.74e-68 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 216.07 E-value: 1.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILR 114
Cdd:PRK11559 5 VGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGIIE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQ 194
Cdd:PRK11559 85 GAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 195 VGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEGvpsanNYQGGFITTL 274
Cdd:PRK11559 165 IGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIR--GGLAGSTVLDAKAPMVMDR-----NFKPGFRIDL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50417829 275 MAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQF 322
Cdd:PRK11559 238 HIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACY 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
35-193 |
2.72e-61 |
|
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: 192.68 E-value: 2.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSnSILR 114
Cdd:pfam03446 2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCG 193
Cdd:pfam03446 81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| tartro_sem_red |
TIGR01505 |
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
35-323 |
2.20e-58 |
|
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: 189.72 E-value: 2.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILR 114
Cdd:TIGR01505 2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGIIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQ 194
Cdd:TIGR01505 82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 195 VGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNmsSGRCWSSDTYNPVPGVMEgvpsaNNYQGGFITTL 274
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALR--GGLAGSTVLEVKGERVID-----RTFKPGFRIDL 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 50417829 275 MAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFL 323
Cdd:TIGR01505 235 HQKDLNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQAL 283
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
35-324 |
2.17e-46 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 158.87 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILR 114
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQ 194
Cdd:PRK15461 84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 195 VGSGQAAKICNN-MLLAIGMLgTAETMNLGIRLGLDPKLLAKILN-MSSGRCWSSDTYnpvPG-VMEGVPSAnnyqgGFI 271
Cdd:PRK15461 164 PGMGIRVKLINNyMSIALNAL-SAEAAVLCEALGLSFDVALKVMSgTAAGKGHFTTTW---PNkVLKGDLSP-----AFM 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 50417829 272 TTLMAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFLR 324
Cdd:PRK15461 235 IDLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
35-323 |
5.09e-41 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 144.78 E-value: 5.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPEScKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTGSNSILR 114
Cdd:PRK15059 3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 115 KVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMGANVVYCGQ 194
Cdd:PRK15059 82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 195 VGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLL----------AKILNMSSGRCWSSdTYNPvpgvmegvpsan 264
Cdd:PRK15059 162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVrqalmggfasSRILEVHGERMIKR-TFNP------------ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 50417829 265 nyqgGFITTLMAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFL 323
Cdd:PRK15059 229 ----GFKIALHQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
29-319 |
4.14e-39 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 147.31 E-value: 4.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 29 MASKTP--VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVY 106
Cdd:PLN02858 319 MQAKPVkrIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 107 TGSNSILRKVKKGTLLIDSSTIDPA-VSK-EMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTC 184
Cdd:PLN02858 399 FGDLGAVSALPAGASIVLSSTVSPGfVIQlERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 185 MGANV-VYCGQVGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDtyNPVPGVMEgvpsa 263
Cdd:PLN02858 479 LSEKLyVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFE--NRVPHMLD----- 551
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 50417829 264 NNYQGGFITTLMAKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSV 319
Cdd:PLN02858 552 NDYTPYSALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAV 607
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
29-301 |
2.57e-35 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 136.13 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 29 MASKTPVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEVYTG 108
Cdd:PLN02858 1 AQSAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 109 SNSILRKVKKGTLLIDSSTIDPA-VSK-EMAVAAEKMGAVFMDAPVSGGVGAASLAKLTFLVGGVEEEYNAAQELLTCMG 186
Cdd:PLN02858 81 DEGAAKGLQKGAVILIRSTILPLqLQKlEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 187 ANV-VYCGQVGSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSsdTYNPVPGVMEGvpsaNN 265
Cdd:PLN02858 161 QKLyTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWI--FKNHVPLLLKD----DY 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 50417829 266 YQGGFITTLmAKDLGFAQNTATSTRTPIPLGSLAHQ 301
Cdd:PLN02858 235 IEGRFLNVL-VQNLGIVLDMAKSLPFPLPLLAVAHQ 269
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
196-323 |
4.92e-33 |
|
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: 118.40 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 196 GSGQAAKICNNMLLAIGMLGTAETMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYnpvpgvMEGVPSANNYQGGFITTLM 275
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENK------FPQRVLSRDFDPGFALDLM 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 50417829 276 AKDLGFAQNTATSTRTPIPLGSLAHQVYRTMCARGYSNKDFSSVFQFL 323
Cdd:pfam14833 75 LKDLGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
35-212 |
9.20e-19 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 84.76 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEK--ADRII-TMLPSSP---NVIEvytg 108
Cdd:COG1023 3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKlpAPRVVwLMVPAGEitdQVIE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 109 snSILRKVKKGTLLID---SSTIDpavSKEMAVAAEKMGAVFMDAPVSGGV-----GAAslakltFLVGGVEEEYNAAQE 180
Cdd:COG1023 79 --ELAPLLEPGDIVIDggnSNYKD---DIRRAEELAEKGIHFVDVGTSGGVwglenGYC------LMIGGDKEAVERLEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50417829 181 LLT--CMGAN--VVYCGQVGSGQAAKICNN-----MLLAIG 212
Cdd:COG1023 148 IFKalAPGAEngYLHCGPVGAGHFVKMVHNgieygMMQAYA 188
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
35-212 |
9.81e-18 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 82.10 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSPAEVAEK--ADRII-TMLPSSP---NVIEvytg 108
Cdd:PRK09599 3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKlpAPRVVwLMVPAGEitdATID---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 109 snSILRKVKKGTLLID---SSTIDpavSKEMAVAAEKMGAVFMDAPVSGGV-----GAAslakltFLVGGVEEEYNAAQE 180
Cdd:PRK09599 79 --ELAPLLSPGDIVIDggnSYYKD---DIRRAELLAEKGIHFVDVGTSGGVwglerGYC------LMIGGDKEAVERLEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 50417829 181 LLTCMGANV----VYCGQVGSGQAAKICNN-----MLLAIG 212
Cdd:PRK09599 148 IFKALAPRAedgyLHAGPVGAGHFVKMVHNgieygMMQAYA 188
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
35-93 |
2.34e-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: 57.00 E-value: 2.34e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYP---VIATDAFPESCKELQD-SGAQILDSPAEVAEKADRII 93
Cdd:COG0345 5 IGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAErYGVRVTTDNAEAAAQADVVV 67
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
31-93 |
2.71e-07 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 50.91 E-value: 2.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50417829 31 SKTPVGFIGLGNMGTPMARNLLKNGYP---VIATDAFPESCKEL-QDSGAQILDSPAEVAEKADRII 93
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALaEEYGVRAATDNQEAAQEADVVV 67
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
35-192 |
4.45e-06 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 47.43 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYP--VIATDAFPESCKELQDSGA--QILDSPAEVAEKADRII--TMLPSSPNVIEvytg 108
Cdd:COG0287 4 IAIIGLGLIGGSLALALKRAGLAheVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVlaVPVGATIEVLA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 109 snSILRKVKKGTLLID-SSTIDPAVskEMAVAAEKMGAVFmdapVSG---------GVGAASL-----AK--LTFLVGGV 171
Cdd:COG0287 80 --ELAPHLKPGAIVTDvGSVKGAVV--EAAEALLPDGVRF----VGGhpmagteksGPEAADAdlfegAPyiLTPTEGTD 151
|
170 180
....*....|....*....|.
gi 50417829 172 EEEYNAAQELLTCMGANVVYC 192
Cdd:COG0287 152 PEALERVEELWEALGARVVEM 172
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
36-124 |
6.24e-05 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 41.06 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 36 GFIGLGNMGTPMARNLLKNGYP--VIATDAFPESCKELQDS---GAQILDsPAEVAEKADRIITMLPssPnviEVYTGSN 110
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEKAEELAEEygvGATAVD-NEEAAEEADVVFLAVK--P---EDAPDVL 74
|
90
....*....|....
gi 50417829 111 SILRKVKKGTLLID 124
Cdd:pfam03807 75 SELSDLLKGKIVIS 88
|
|
| PTZ00142 |
PTZ00142 |
6-phosphogluconate dehydrogenase; Provisional |
35-206 |
7.78e-05 |
|
6-phosphogluconate dehydrogenase; Provisional
Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 44.01 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIA-------TDAFPESCKE--LQDSGAQILDSPAEVAEKADRIITMLPSSPNVIEV 105
Cdd:PTZ00142 4 IGLIGLAVMGQNLALNIASRGFKISVynrtyekTEEFVKKAKEgnTRVKGYHTLEELVNSLKKPRKVILLIKAGEAVDET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 106 YtgsNSILRKVKKGTLLIDSSTIDPAVSKEMAVAAEKMGAVFMDAPVSGGVGAASLAKlTFLVGGVEEEYNAAQELLTCM 185
Cdd:PTZ00142 84 I---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKC 159
|
170 180
....*....|....*....|....*..
gi 50417829 186 GANV------VYCGQVGSGQAAKICNN 206
Cdd:PTZ00142 160 SAKVgdspcvTYVGPGSSGHYVKMVHN 186
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
35-104 |
1.47e-04 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 42.64 E-value: 1.47e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPV-----IATDAFPESCKELQDSGAQILDSPAEVAEKADRIItmLPSSPNVIE 104
Cdd:PLN02688 3 VGFIGAGKMAEAIARGLVASGVVPpsrisTADDSNPARRDVFQSLGVKTAASNTEVVKSSDVII--LAVKPQVVK 75
|
|
| LDH_like |
cd01619 |
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ... |
1-126 |
1.67e-04 |
|
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: 42.67 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 1 MAALFRGYRNFYKRSNKHVELIL-VSCRSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEscKELQDSGAQiL 79
Cdd:cd01619 112 ILALLRNRKYIDERDKNQDLQDAgVIGRELEDQT-VGVVGTGKIGRAVAQRAKGFGMKVIAYDPFRN--PELEDKGVK-Y 187
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 50417829 80 DSPAEVAEKADrIITM-LPSSPNVIEVYTGSNsiLRKVKKGTLLIDSS 126
Cdd:cd01619 188 VSLEELFKNSD-IISLhVPLTPENHHMINEEA--FKLMKKGVIIINTA 232
|
|
| PGDH_like_2 |
cd12172 |
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
27-123 |
2.36e-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: 42.09 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 27 RSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPEScKELQDSGAQILdSPAEVAEKADRIITMLPSSP---NVI 103
Cdd:cd12172 138 TELYGKT-LGIIGLGRIGKAVARRLSGFGMKVLAYDPYPDE-EFAKEHGVEFV-SLEELLKESDFISLHLPLTPetrHLI 214
|
90 100
....*....|....*....|
gi 50417829 104 evytgSNSILRKVKKGTLLI 123
Cdd:cd12172 215 -----NAAELALMKPGAILI 229
|
|
| 2-Hacid_dh_C |
pfam02826 |
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ... |
1-123 |
2.98e-04 |
|
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.
Pssm-ID: 427007 [Multi-domain] Cd Length: 178 Bit Score: 40.94 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 1 MAALFRGYRNFYK-----RSNKHVELILVSCRSMASKTpVGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSG 75
Cdd:pfam02826 1 LALLLALARRIPEadrqvRAGRWASPDALLGRELSGKT-VGIIGLGRIGRAVAKRLKAFGMKVIAYDRYPKPEEEEEELG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 50417829 76 AQiLDSPAEVAEKADrIITM-LPSSP---NVIevytgSNSILRKVKKGTLLI 123
Cdd:pfam02826 80 AR-YVSLDELLAESD-VVSLhLPLTPetrHLI-----NAERLALMKPGAILI 124
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
39-140 |
9.57e-04 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 40.74 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 39 GLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDS-GAQILDSPAEVAEKADRIITMLP--SSPNVIEvytgsnSILRK 115
Cdd:PRK08655 8 GTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISVPinVTEDVIK------EVAPH 81
|
90 100
....*....|....*....|....*
gi 50417829 116 VKKGTLLIDSSTIdpavsKEMAVAA 140
Cdd:PRK08655 82 VKEGSLLMDVTSV-----KERPVEA 101
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
38-79 |
1.19e-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: 40.05 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 50417829 38 IGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQIL 79
Cdd:COG0569 101 IGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVI 142
|
|
| PTDH |
cd12157 |
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ... |
35-140 |
1.83e-03 |
|
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: 39.58 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417829 35 VGFIGLGNMGTPMARNLLKNGYPVIATDAFPESCKELQDSGAQILDSpAEVAEKADRIITMLPSSPNVIEVYTGSNsiLR 114
Cdd:cd12157 147 VGILGMGALGRAIARRLSGFGATLLYYDPHPLDQAEEQALNLRRVEL-DELLESSDFLVLALPLTPDTLHLINAEA--LA 223
|
90 100
....*....|....*....|....*.
gi 50417829 115 KVKKGTLLIDSSTidPAVSKEMAVAA 140
Cdd:cd12157 224 KMKPGALLVNPCR--GSVVDEAAVAE 247
|
|
| |
