|
Name |
Accession |
Description |
Interval |
E-value |
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-296 |
0e+00 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 584.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 1 MTIKVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 81 GIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
Cdd:PRK11559 81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1462009253 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVTR 296
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
|
|
| tartro_sem_red |
TIGR01505 |
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
4-294 |
2.42e-165 |
|
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: 460.51 E-value: 2.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505 1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505 81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 164 DIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1462009253 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
4-286 |
2.68e-126 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 361.36 E-value: 2.68e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:COG2084 83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 164 DIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:COG2084 163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1462009253 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084 243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-163 |
2.05e-66 |
|
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: 204.63 E-value: 2.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
19-115 |
1.27e-03 |
|
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214967 [Multi-domain] Cd Length: 133 Bit Score: 38.16 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 19 KNLLKAGYSLVV----------SDrnpeaiADVIAAGAETATTPKAVAeQCDVIItmlpnspHVKEVALGEngiIEGAKP 88
Cdd:smart01003 21 KKLVKLGHEVLVesgagegagfSD------EAYEAAGAEIVDTAEVWA-DADIIL-------KVKEPSPEE---LALLRE 83
|
90 100
....*....|....*....|....*..
gi 1462009253 89 GTVVIDMssIAPLASREISEALKAKGI 115
Cdd:smart01003 84 GQILFGY--LHPAANPELLEALAAKGV 108
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-296 |
0e+00 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 584.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 1 MTIKVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 81 GIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
Cdd:PRK11559 81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1462009253 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVTR 296
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEVTR 296
|
|
| tartro_sem_red |
TIGR01505 |
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ... |
4-294 |
2.42e-165 |
|
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: 460.51 E-value: 2.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505 1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505 81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 164 DIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1462009253 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
4-286 |
2.68e-126 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 361.36 E-value: 2.68e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:COG2084 83 AALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 164 DIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:COG2084 163 DAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDLG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1462009253 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084 243 LALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
3-290 |
7.47e-78 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 238.77 E-value: 7.47e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 3 IKVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAiADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGI 82
Cdd:PRK15059 1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 83 IEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162
Cdd:PRK15059 80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 163 GDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1462009253 243 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLA 290
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMA 287
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-163 |
2.05e-66 |
|
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: 204.63 E-value: 2.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
7-286 |
5.80e-66 |
|
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: 208.11 E-value: 5.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 7 FIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGIIEGA 86
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 87 KPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGDIG 166
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 167 AGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFRIDLHI 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVpgVMPqapasNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1462009253 240 KDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-282 |
3.62e-61 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 195.85 E-value: 3.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:PRK15461 83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 164 DIGAGNVTKLANQVI-VALNiAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKD 241
Cdd:PRK15461 163 GPGMGIRVKLINNYMsIALN-ALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1462009253 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSAL 282
Cdd:PRK15461 242 LGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAI 282
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
166-286 |
1.55e-45 |
|
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: 149.98 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 166 GAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKDLAN 244
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1462009253 245 ALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
4-294 |
9.05e-39 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 144.99 E-value: 9.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PLN02858 326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEALKA--KGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSV-V 160
Cdd:PLN02858 406 SALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PLN02858 486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1462009253 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:PLN02858 566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKV 619
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
4-295 |
8.35e-35 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 133.44 E-value: 8.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PLN02858 6 VVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 84 EGAKPGTVVIDMSSIAPLASREISEAL--KAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSV-V 160
Cdd:PLN02858 86 KGLQKGAVILIRSTILPLQLQKLEKKLteRKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLyT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PLN02858 166 FEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQ 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1462009253 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVT 295
Cdd:PLN02858 246 NLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNIL 300
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
4-173 |
1.08e-23 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 97.85 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCD---VIITMLPNSPHVKEVaLGEn 80
Cdd:COG1023 2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQV-IEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 81 gIIEGAKPGTVVID------MSSIAplasReiSEALKAKGIDMLDAPVSGGepkaIDGTL---SVMVGGDKAIFDKYYDL 151
Cdd:COG1023 80 -LAPLLEPGDIVIDggnsnyKDDIR----R--AEELAEKGIHFVDVGTSGG----VWGLEngyCLMIGGDKEAVERLEPI 148
|
170 180
....*....|....*....|....*.
gi 1462009253 152 MKAMA----GSVVHTGDIGAGNVTKL 173
Cdd:COG1023 149 FKALApgaeNGYLHCGPVGAGHFVKM 174
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
4-172 |
1.95e-22 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 94.43 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVAEQCD---VIITMLPNSPHVKEVAlgeN 80
Cdd:PRK09599 2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI---D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 81 GIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGepkaIDGTL---SVMVGGDKAIFDKYYDLMKAMA- 156
Cdd:PRK09599 79 ELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGG----VWGLErgyCLMIGGDKEAVERLEPIFKALAp 154
|
170
....*....|....*....
gi 1462009253 157 ---GSVVHTGDIGAGNVTK 172
Cdd:PRK09599 155 raeDGYLHAGPVGAGHFVK 173
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-99 |
2.79e-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: 56.61 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 1 MTIKVGFIGLGIMGKPMSKNLLKAGYS---LVVSDRNPEAIADVIAA-GAETATTPKAVAEQCDVII-TMLPNspHVKEV 75
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVlAVKPQ--DLAEV 78
|
90 100
....*....|....*....|....
gi 1462009253 76 AlgeNGIIEGAKPGTVVIdmsSIA 99
Cdd:COG0345 79 L---EELAPLLDPDKLVI---SIA 96
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-63 |
1.05e-07 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 52.07 E-value: 1.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1462009253 1 MTIKVGFIGLGIMGKPMSKNLLKAGYS---LVVSDRNPEAIADVIAA-GAETATTPKAVAEQCDVII 63
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
5-94 |
1.99e-07 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 50.55 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 5 VGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAA--GAETATTPKAVAEQCDVIITMLPNSpHVKEVAlgenGI 82
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAElgPGARAGTNAEAAAAADVVVLAVPYE-AVPDVL----ES 75
|
90
....*....|..
gi 1462009253 83 IEGAKPGTVVID 94
Cdd:COG2085 76 LGDALAGKIVID 87
|
|
| PTZ00142 |
PTZ00142 |
6-phosphogluconate dehydrogenase; Provisional |
5-192 |
7.62e-07 |
|
6-phosphogluconate dehydrogenase; Provisional
Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 50.17 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 5 VGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTPKAVA---------EQCDVIITMLPNSPHVKEV 75
Cdd:PTZ00142 4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKKAKEGNTRVKGYHtleelvnslKKPRKVILLIKAGEAVDET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 76 AlgeNGIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLMKAM 155
Cdd:PTZ00142 84 I---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKC 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1462009253 156 AGSV------VHTGDIGAGNVTKLANQVIVALNIAAMSEALTL 192
Cdd:PTZ00142 160 SAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKL 202
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
4-98 |
8.76e-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: 46.27 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAG--YSLVVSDRNPEAIADVIAAGA--ETATTPKAVAEQCDVIITMLPnsphVKEVA--L 77
Cdd:COG0287 3 RIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELGVidRAATDLEEAVADADLVVLAVP----VGATIevL 78
|
90 100
....*....|....*....|.
gi 1462009253 78 GEngIIEGAKPGTVVIDMSSI 98
Cdd:COG0287 79 AE--LAPHLKPGAIVTDVGSV 97
|
|
| PLN02350 |
PLN02350 |
phosphogluconate dehydrogenase (decarboxylating) |
4-173 |
1.70e-05 |
|
phosphogluconate dehydrogenase (decarboxylating)
Pssm-ID: 215200 [Multi-domain] Cd Length: 493 Bit Score: 45.86 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAAGAETATTP-----------KAVAEQCDVIITMLPNSPhv 72
Cdd:PLN02350 8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVERAKKEGNLPlygfkdpedfvLSIQKPRSVIILVKAGAP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 73 keVALGENGIIEGAKPGTVVIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLM 152
Cdd:PLN02350 86 --VDQTIKALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDIL 162
|
170 180
....*....|....*....|....*..
gi 1462009253 153 KAMAGS------VVHTGDIGAGNVTKL 173
Cdd:PLN02350 163 EKVAAQvddgpcVTYIGPGGAGNFVKM 189
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
3-162 |
4.40e-05 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 44.59 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 3 IKVGFIG-LGIMGKPMSKNLLKAGYSLVVSDRNPEAIADVIAA-GAETATTPKAVAEQCDVIITMLP---NSPHVKEVAl 77
Cdd:PRK08655 1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISVPinvTEDVIKEVA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 78 gengiiEGAKPGTVVIDMSSIAPLASREISEALKaKGIDMLDA-PVSGGEPKAIDGTLSVMV---GGDKAIFDKYYDLMK 153
Cdd:PRK08655 80 ------PHVKEGSLLMDVTSVKERPVEAMEEYAP-EGVEILPThPMFGPRTPSLKGQVVILTpteKRSNPWFDKVKNFLE 152
|
....*....
gi 1462009253 154 AMAGSVVHT 162
Cdd:PRK08655 153 KEGARVIVT 161
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
19-115 |
9.54e-05 |
|
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 461595 [Multi-domain] Cd Length: 135 Bit Score: 41.64 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 19 KNLLKAGYSLVVSDRNPEAI----ADVIAAGAETATTPKAVAEQCDVIItmlpnspHVKEVALGEngiIEGAKPGTVVID 94
Cdd:pfam05222 21 KKLVKLGHEVLVESGAGLGAgfsdEAYEAAGAEIVDTAAEVWAEADLIL-------KVKEPQPEE---YALLREGQTLIT 90
|
90 100
....*....|....*....|.
gi 1462009253 95 MssIAPLASREISEALKAKGI 115
Cdd:pfam05222 91 F--LHPAANPELLEALAAKGV 109
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
6-96 |
1.37e-04 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 39.91 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 6 GFIGLGIMGKPMSKNLLKAGYS--LVVSDRNPE---AIADVIAAGAeTATTPKAVAEQCDVIITMLPnsPHVKEVALGEn 80
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEkaeELAEEYGVGA-TAVDNEEAAEEADVVFLAVK--PEDAPDVLSE- 76
|
90
....*....|....*.
gi 1462009253 81 giIEGAKPGTVVIDMS 96
Cdd:pfam03807 77 --LSDLLKGKIVISIA 90
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-77 |
3.35e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 41.45 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 1 MTIKVGFIGLGIMGKPMSKNLLK-AGYSLV-VSDRNPEAIADVIAA-GAETATTPKAVAEQCD---VIITmLPNSPHVkE 74
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAAlPGVELVaVADRDPERAEAFAEEyGVRVYTDYEELLADPDidaVVIA-TPNHLHA-E 79
|
...
gi 1462009253 75 VAL 77
Cdd:COG0673 80 LAI 82
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
19-115 |
1.27e-03 |
|
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214967 [Multi-domain] Cd Length: 133 Bit Score: 38.16 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1462009253 19 KNLLKAGYSLVV----------SDrnpeaiADVIAAGAETATTPKAVAeQCDVIItmlpnspHVKEVALGEngiIEGAKP 88
Cdd:smart01003 21 KKLVKLGHEVLVesgagegagfSD------EAYEAAGAEIVDTAEVWA-DADIIL-------KVKEPSPEE---LALLRE 83
|
90 100
....*....|....*....|....*..
gi 1462009253 89 GTVVIDMssIAPLASREISEALKAKGI 115
Cdd:smart01003 84 GQILFGY--LHPAANPELLEALAAKGV 108
|
|
| |
