|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
33-318 |
6.92e-119 |
|
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: 344.09 E-value: 6.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 33 FVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASY--DEMTADGV 110
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYsgDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 111 NKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGVYG 190
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 191 MGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPVPGVCPSAPANRDYAGGFSSALIT 270
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24655230 271 KDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMK 318
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
29-317 |
3.02e-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: 3.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMT-- 106
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 107 ADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHC 186
Cdd:COG2084 82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 187 GVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPvpgvcpsAPANRDYAGGFSS 266
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24655230 267 ALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLM 317
Cdd:COG2084 235 DLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
30-187 |
6.22e-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: 196.54 E-value: 6.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMT-AD 108
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGlLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655230 109 GVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCG 187
Cdd:pfam03446 81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
29-311 |
2.72e-59 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 192.19 E-value: 2.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDA--SYDEMT 106
Cdd:PRK11559 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEvaLGENGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 107 ADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHC 186
Cdd:PRK11559 83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 187 GVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDA-NVFAEIINSSTGrcwaSEIYNP-VPGVcpsapANRDYAGGF 264
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPdLVYQAIRGGLAG----STVLDAkAPMV-----MDRNFKPGF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24655230 265 SSALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFS 311
Cdd:PRK11559 234 RIDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHS 280
|
|
| 2-Hacid_dh_9 |
cd12170 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
30-154 |
8.39e-05 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 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: 240647 [Multi-domain] Cd Length: 294 Bit Score: 43.44 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLHVFDIS-KPACDglaAKGATvYAKTSELAKNSDFVITMLPNNAIVdASYDEMTAD 108
Cdd:cd12170 140 KVGIIGLGTTGQMIADALSFFGADVYYYSRTrKPDAE---AKGIR-YLPLNELLKTVDVICTCLPKNVIL-LGEEEFELL 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24655230 109 GVNKdtIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAE 154
Cdd:cd12170 215 GDGK--ILFNTSLGPSFEVEALKKWLKASGYNIFDCDTAGALGDEE 258
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
33-318 |
6.92e-119 |
|
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: 344.09 E-value: 6.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 33 FVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASY--DEMTADGV 110
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYsgDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 111 NKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGVYG 190
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 191 MGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPVPGVCPSAPANRDYAGGFSSALIT 270
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVPGVMPQAPASNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 24655230 271 KDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMK 318
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLLR 288
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
29-317 |
3.02e-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: 3.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMT-- 106
Cdd:COG2084 2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 107 ADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHC 186
Cdd:COG2084 82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 187 GVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPvpgvcpsAPANRDYAGGFSS 266
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGP-------RMLAGDFDPGFAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24655230 267 ALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLM 317
Cdd:COG2084 235 DLMLKDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
30-187 |
6.22e-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: 196.54 E-value: 6.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASYDEMT-AD 108
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGlLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655230 109 GVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCG 187
Cdd:pfam03446 81 GLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
29-311 |
2.72e-59 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 192.19 E-value: 2.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDA--SYDEMT 106
Cdd:PRK11559 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEvaLGENGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 107 ADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHC 186
Cdd:PRK11559 83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 187 GVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDA-NVFAEIINSSTGrcwaSEIYNP-VPGVcpsapANRDYAGGF 264
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPdLVYQAIRGGLAG----STVLDAkAPMV-----MDRNFKPGF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 24655230 265 SSALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFS 311
Cdd:PRK11559 234 RIDLHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHS 280
|
|
| tartro_sem_red |
TIGR01505 |
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
31-321 |
2.41e-56 |
|
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: 184.32 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDA-SYDEM-TAD 108
Cdd:TIGR01505 2 VGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEvAFGENgIIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 109 GVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGV 188
Cdd:TIGR01505 82 GAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 189 YGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEIYNPVpgvcpsaPANRDYAGGFSSAL 268
Cdd:TIGR01505 162 NGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGER-------VIDRTFKPGFRIDL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 24655230 269 ITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVV---YDLMKKEK 321
Cdd:TIGR01505 235 HQKDLNLALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALvqaLELLANHK 290
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
31-318 |
4.28e-51 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 170.81 E-value: 4.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASY--DEMTAD 108
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLfgENGVCE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 109 GVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGV 188
Cdd:PRK15461 84 GLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 189 YGMGQAAKLCNNMMlAISMIGVS-EAMNLAVRQGLDANVFAEIIN-SSTGRCWASEIYnpvpgvcPSAPANRDYAGGFSS 266
Cdd:PRK15461 164 PGMGIRVKLINNYM-SIALNALSaEAAVLCEALGLSFDVALKVMSgTAAGKGHFTTTW-------PNKVLKGDLSPAFMI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 24655230 267 ALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMK 318
Cdd:PRK15461 236 DLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVR 287
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
31-323 |
4.22e-40 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 142.08 E-value: 4.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVFDISkPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIV-DASYDEM-TAD 108
Cdd:PRK15059 3 LGFIGLGIMGTPMAINLARAGHQLHVTTIG-PVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVeEVLFGENgCTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 109 GVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKITHCGV 188
Cdd:PRK15059 82 ASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 189 YGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDAnvfAEIINSSTGRCWASEIYNpvpgVCPSAPANRDYAGGFSSAL 268
Cdd:PRK15059 162 NGDGQTCKVANQIIVALNIEAVSEALLFASKAGADP---VRVRQALMGGFASSRILE----VHGERMIKRTFNPGFKIAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24655230 269 ITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVV---YDLMKKEKFS 323
Cdd:PRK15059 235 HQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALvqaLELMANHKLA 292
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
28-313 |
7.91e-38 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 143.45 E-value: 7.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 28 AKNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASY--DEM 105
Cdd:PLN02858 324 VKRIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLfgDLG 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 106 TADGVNKDTIFIDSSTISPDLVKSLQKKISA--KGARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKI 183
Cdd:PLN02858 404 AVSALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKL 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 184 THC-GVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEiyNPVPGVCpsapaNRDYAG 262
Cdd:PLN02858 484 YVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFE--NRVPHML-----DNDYTP 556
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24655230 263 GFSSALITKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVV 313
Cdd:PLN02858 557 YSALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAV 607
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
190-314 |
2.02e-34 |
|
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: 121.86 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 190 GMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWASEiynpvpGVCPSAPANRDYAGGFSSALI 269
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALE------NKFPQRVLSRDFDPGFALDLM 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24655230 270 TKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVY 314
Cdd:pfam14833 75 LKDLGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAII 119
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
28-319 |
4.36e-30 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 120.73 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 28 AKNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDASY--DEM 105
Cdd:PLN02858 4 AGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFfgDEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 106 TADGVNKDTIFIDSSTISPDLVKSLQKKISAKG--ARFIDAPVSGGVPGAEQATLTFMVGGTEAEYNAVKAVLECMGKKI 183
Cdd:PLN02858 84 AAKGLQKGAVILIRSTILPLQLQKLEKKLTERKeqIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 184 -THCGVYGMGQAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANVFAEIINSSTGRCWaseIY-NPVPGVCPSAPANRDYA 261
Cdd:PLN02858 164 yTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSW---IFkNHVPLLLKDDYIEGRFL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24655230 262 GGFSsalitKDLGLASGVANASNSPIPLGSLAHKVYQSLCDKGLGNKDFSVVYDLMKK 319
Cdd:PLN02858 241 NVLV-----QNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEK 293
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
31-205 |
1.59e-22 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 95.16 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSD---FVITMLPNNAIVDASYDEMTA 107
Cdd:COG1023 3 IGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQVIEELAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 108 ---------DGVN---KDTIfidsstispdlvkSLQKKISAKGARFIDAPVSGGVPGAEQAtLTFMVGGTEAEYNAVKAV 175
Cdd:COG1023 83 llepgdiviDGGNsnyKDDI-------------RRAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPI 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 24655230 176 LE--CMGKK--ITHCGVYGMGQAAKLCNN-----MMLAI 205
Cdd:COG1023 149 FKalAPGAEngYLHCGPVGAGHFVKMVHNgieygMMQAY 187
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
31-194 |
1.77e-22 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 95.20 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVFDISKPACDGLAAKGATVYAKTSELAKNSD---FVITMLPNNAIVDASYDEMtA 107
Cdd:PRK09599 3 LGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATIDEL-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 108 DGVNKDTIFIDS--STISPDLVKSlqKKISAKGARFIDAPVSGGVPGAEQAtLTFMVGGTEAEYNAVKAVLEC------- 178
Cdd:PRK09599 82 PLLSPGDIVIDGgnSYYKDDIRRA--ELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKAlapraed 158
|
170 180
....*....|....*....|....*...
gi 24655230 179 ----MGK-------KITHCGV-YGMGQA 194
Cdd:PRK09599 159 gylhAGPvgaghfvKMVHNGIeYGMMQA 186
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
29-89 |
2.13e-08 |
|
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: 54.30 E-value: 2.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHK---LHVFDISKPACDGLAAK-GATVYAKTSELAKNSDFVI 89
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVV 67
|
|
| PRK09287 |
PRK09287 |
NADP-dependent phosphogluconate dehydrogenase; |
39-177 |
9.39e-06 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236453 [Multi-domain] Cd Length: 459 Bit Score: 47.04 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 39 MGANMASNLIKAGHKLHVFDISKPACDGLAA---KGATVYAkTSELAknsDFV---------ITMLPNNAIVDASYDEMt 106
Cdd:PRK09287 1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAeegKGKKIVP-AYTLE---EFVaslekprkiLLMVKAGAPVDAVIEQL- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655230 107 ADGVNKDTIFIDS-STISPDLVKSLqKKISAKGARFIDAPVSGGVPGAeqatLT---FMVGGTEAEYNAVKAVLE 177
Cdd:PRK09287 76 LPLLEKGDIIIDGgNSNYKDTIRRE-KELAEKGIHFIGMGVSGGEEGA----LHgpsIMPGGQKEAYELVAPILE 145
|
|
| PTZ00142 |
PTZ00142 |
6-phosphogluconate dehydrogenase; Provisional |
30-216 |
2.31e-05 |
|
6-phosphogluconate dehydrogenase; Provisional
Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 45.93 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLHVFDISKPACD----GLAAKGATVYA-KTSELAKNS----DFVITMLPNNAIVDA 100
Cdd:PTZ00142 3 DIGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEefvkKAKEGNTRVKGyHTLEELVNSlkkpRKVILLIKAGEAVDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 101 SYDEMTADgVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAEQATlTFMVGGTEAEYNAVKAVLECMG 180
Cdd:PTZ00142 83 TIDNLLPL-LEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKCS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 24655230 181 KKI------THCGVYGMGQAAKLCNNMMLAISMIGVSEAMNL 216
Cdd:PTZ00142 161 AKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKL 202
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
31-181 |
3.38e-05 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 44.56 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAG----HKLHVFDISKPA-CDGLAAKGATVYAKTSELAKNSDFVITMLPNNAIVDAsYDEM 105
Cdd:PLN02688 3 VGFIGAGKMAEAIARGLVASGvvppSRISTADDSNPArRDVFQSLGVKTAASNTEVVKSSDVIILAVKPQVVKDV-LTEL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24655230 106 TADgVNKDTIFIdsSTISPDLVKSLQKkiSAKGARFIDapVSGGVPGAEQATLTFMVGG---TEAEYNAVKAVLECMGK 181
Cdd:PLN02688 82 RPL-LSKDKLLV--SVAAGITLADLQE--WAGGRRVVR--VMPNTPCLVGEAASVMSLGpaaTADDRDLVATLFGAVGK 153
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
29-89 |
4.33e-05 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 44.37 E-value: 4.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAG---HKLHVFDISKPACDGLAAK-GATVYAKTSELAKNSDFVI 89
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
|
|
| 2-Hacid_dh_9 |
cd12170 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
30-154 |
8.39e-05 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 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: 240647 [Multi-domain] Cd Length: 294 Bit Score: 43.44 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLHVFDIS-KPACDglaAKGATvYAKTSELAKNSDFVITMLPNNAIVdASYDEMTAD 108
Cdd:cd12170 140 KVGIIGLGTTGQMIADALSFFGADVYYYSRTrKPDAE---AKGIR-YLPLNELLKTVDVICTCLPKNVIL-LGEEEFELL 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 24655230 109 GVNKdtIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGVPGAE 154
Cdd:cd12170 215 GDGK--ILFNTSLGPSFEVEALKKWLKASGYNIFDCDTAGALGDEE 258
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
29-250 |
1.06e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 43.75 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHVFDISK---------------PA-----CDGLAAKGATVYAKTSELAKNSDFV 88
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQekvdklnkgkspiyePGldellAKALKAGRLRATTDYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 89 ITMLPNNAIVDASYD--------EMTADGVNKDTIFIDSSTISPDLVKSLQKKISAKGARFIDAPVSGGV------PGAE 154
Cdd:TIGR03026 81 IICVPTPLKEDGSPDlsyvesaaETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDFYLAYnpeflrEGNA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 155 QATLTF---MVGG-TEAEYNAVKAVLEcmgkKITHCGVYGMG----QAAKLCNNMMLAISMIGVSEAMNLAVRQGLDANV 226
Cdd:TIGR03026 161 VHDLLHpdrIVGGeTEEAGEAVAELYS----PIIDGPVLVTSietaEMIKLAENTFRAVKIAFANELARICEALGIDVYE 236
|
250 260
....*....|....*....|....
gi 24655230 227 FAEIINssTGRCWASEIYNPVPGV 250
Cdd:TIGR03026 237 VIEAAG--TDPRIGFNFLNPGPGV 258
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
30-97 |
1.18e-04 |
|
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];
Pssm-ID: 444246 [Multi-domain] Cd Length: 286 Bit Score: 42.88 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 30 NIGFVGLGNMGANMASNLIKAGHKLH-VFDISKPACDGLAAK-GATVYAKTSELAKNSDFVITMLPNNAI 97
Cdd:COG5495 5 KIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALlGAVPALDLEELAAEADLVLLAVPDDAI 74
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
31-118 |
2.33e-03 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 38.61 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 31 IGFVGLGNMGANMASNLIKAGHKLHVF--DISKpACDGLAAKGATVYAKT-SELAKNSDFVITMLPNNAIVDAsyDEMTA 107
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVIGsrDPEK-AAALAAELGPGARAGTnAEAAAAADVVVLAVPYEAVPDV--LESLG 77
|
90
....*....|.
gi 24655230 108 DGVnKDTIFID 118
Cdd:COG2085 78 DAL-AGKIVID 87
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
29-155 |
3.73e-03 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 38.57 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 29 KNIGFVGLGNMGANMASNLIKAGHKLHV--FDISKPACD-----GLAAKGATVYAktsELAKNSDFVITMLPNNAIVDAs 101
Cdd:COG0287 2 MRIAIIGLGLIGGSLALALKRAGLAHEVvgVDRSPETLEralelGVIDRAATDLE---EAVADADLVVLAVPVGATIEV- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 24655230 102 YDEMtADGVNKDTIFID-SSTISPdLVKSLqKKISAKGARFIdapvsGGVP--GAEQ 155
Cdd:COG0287 78 LAEL-APHLKPGAIVTDvGSVKGA-VVEAA-EALLPDGVRFV-----GGHPmaGTEK 126
|
|
| Mand_dh_like |
cd12168 |
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified ... |
14-96 |
4.98e-03 |
|
D-Mandelate Dehydrogenase-like dehydrogenases; D-Mandelate dehydrogenase (D-ManDH), identified as an enzyme that interconverts benzoylformate and D-mandelate, is a D-2-hydroxyacid dehydrogenase family member that catalyzes the conversion of c3-branched 2-ketoacids. D-ManDH exhibits broad substrate specificities for 2-ketoacids with large hydrophobic side chains, particularly those with C3-branched side chains. 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. Glycerate dehydrogenase catalyzes the reaction (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. 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: 240645 [Multi-domain] Cd Length: 321 Bit Score: 38.30 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24655230 14 WSQTLVRAMSTQGGA----------KNIGFVGLGNMGANMASNLIKAGHKLHVFDISKPAcDGLAAKGATVYAKTSELAK 83
Cdd:cd12168 130 RAERSARAGKWRGFLdltlahdprgKTLGILGLGGIGKAIARKAAAFGMKIIYHNRSRLP-EELEKALATYYVSLDELLA 208
|
90
....*....|...
gi 24655230 84 NSDFVITMLPNNA 96
Cdd:cd12168 209 QSDVVSLNCPLTA 221
|
|
| |
