|
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: 579.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 81 GIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
Cdd:PRK11559 81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 162139755 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 |
6.74e-167 |
|
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: 464.36 E-value: 6.74e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505 1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505 81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 164 EIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 162139755 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
2-286 |
1.50e-124 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 357.12 E-value: 1.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENG 81
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 82 IIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 162 TGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKD 241
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 162139755 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-163 |
6.36e-65 |
|
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: 200.77 E-value: 6.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
19-115 |
3.65e-04 |
|
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: 39.71 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 19 KNLLKAGYSLVVADRNPEAI----ADVIAAGAETASTAKAIAeQCDVIItmlpnspHVKEVALGEngiIEGAKPGTVLID 94
Cdd:smart01003 21 KKLVKLGHEVLVESGAGEGAgfsdEAYEAAGAEIVDTAEVWA-DADIIL-------KVKEPSPEE---LALLREGQILFG 89
|
90 100
....*....|....*....|.
gi 162139755 95 MssIAPLASREISEALKAKGI 115
Cdd:smart01003 90 Y--LHPAANPELLEALAAKGV 108
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
37-179 |
1.71e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 39.31 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 37 AIADVIAAGAETASTAKAIAEQCDVIITMlpNSPHVKEVALgengiiegAKPGTVLIDMSSIAplASREISEALKAKGI- 115
Cdd:cd01620 45 SDEDYLQAGAQIVPAASKEAYSADIIVKL--KEPEFAEYDL--------IKKGQLLVTFLHAA--TNRGVVEVLMRKKLt 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 116 --DMLDAPVSGGEPKAIDGTLSvmvgGDKAIFDKYYDLMKAMAGSVVHTGE--------IGAGNV--------TKLANQV 177
Cdd:cd01620 113 ayALEDLENDFRPRLAPNSNIA----GYAGVQLGAYELARIQGGRMGGAGGvppakvliIGAGVVglgaakiaKKLGANV 188
|
..
gi 162139755 178 IV 179
Cdd:cd01620 189 LV 190
|
|
| |
|
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: 579.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 81 GIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
Cdd:PRK11559 81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 162139755 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 |
6.74e-167 |
|
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: 464.36 E-value: 6.74e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:TIGR01505 1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPEVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:TIGR01505 81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 164 EIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDLA 243
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 162139755 244 NALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
2-286 |
1.50e-124 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 357.12 E-value: 1.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 2 TMKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENG 81
Cdd:COG2084 1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 82 IIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVH 161
Cdd:COG2084 81 LLAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 162 TGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKD 241
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 162139755 242 LANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
3-290 |
1.86e-78 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 240.31 E-value: 1.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAiADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGI 82
Cdd:PRK15059 1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 83 IEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162
Cdd:PRK15059 80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 163 GEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 162139755 243 ANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLA 290
Cdd:PRK15059 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMA 287
|
|
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
7-286 |
3.03e-65 |
|
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: 206.19 E-value: 3.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 7 FIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGIIEGA 86
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 87 KPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTGEIG 166
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 167 AGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPM--VMD-----RNFKPGFRIDLHI 239
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDTYNPVpgVMPqapasNGYQGGFGTALML 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 162139755 240 KDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
4-163 |
6.36e-65 |
|
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: 200.77 E-value: 6.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGEnGII 83
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGE-GLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-282 |
6.80e-60 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 192.76 E-value: 6.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHTG 163
Cdd:PRK15461 83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 164 EIGAGNVTKLANQVI-VALNiAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKD 241
Cdd:PRK15461 163 GPGMGIRVKLINNYMsIALN-ALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPnKVLKGDLSPAFMIDLAHKD 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 162139755 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 |
9.00e-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: 148.06 E-value: 9.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 166 GAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAP-MVMDRNFKPGFRIDLHIKDLAN 244
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFALDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 162139755 245 ALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYY 286
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
4-294 |
8.47e-37 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 139.22 E-value: 8.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGENGII 83
Cdd:PLN02858 326 RIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 84 EGAKPGTVLIDMSSIAPLASREISEALKA--KGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSV-V 160
Cdd:PLN02858 406 SALPAGASIVLSSTVSPGFVIQLERRLENegRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEKLyV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 161 HTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
Cdd:PLN02858 486 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDIFVK 565
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 162139755 241 DLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEV 294
Cdd:PLN02858 566 DLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKV 619
|
|
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
1-295 |
7.28e-34 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 130.74 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCDVIITMLPNSPHVKEVALGEN 80
Cdd:PLN02858 3 SAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 81 GIIEGAKPGTVLIDMSSIAPLASREISEAL--KAKGIDMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGS 158
Cdd:PLN02858 83 GAAKGLQKGAVILIRSTILPLQLQKLEKKLteRKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 159 V-VHTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDL 237
Cdd:PLN02858 163 LyTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 162139755 238 HIKDLANALDTSHGVGAQLPLTAAVMEMMQALRADGLGTADHSALACYYEKLAKVEVT 295
Cdd:PLN02858 243 LVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNIL 300
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
3-173 |
6.07e-24 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 98.62 E-value: 6.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCD---VIITMLPNSPHVKEVaLGE 79
Cdd:COG1023 1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQV-IEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 80 ngIIEGAKPGTVLID------MSSIAplasReiSEALKAKGIDMLDAPVSGGepkaIDGTL---SVMVGGDKAIFDKYYD 150
Cdd:COG1023 80 --LAPLLEPGDIVIDggnsnyKDDIR----R--AEELAEKGIHFVDVGTSGG----VWGLEngyCLMIGGDKEAVERLEP 147
|
170 180
....*....|....*....|....*..
gi 162139755 151 LMKAMA----GSVVHTGEIGAGNVTKL 173
Cdd:COG1023 148 IFKALApgaeNGYLHCGPVGAGHFVKM 174
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
3-172 |
1.37e-22 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 94.82 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAAGAETASTAKAIAEQCD---VIITMLPNSPHVKEVAlge 79
Cdd:PRK09599 1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 80 NGIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGepkaIDGTL---SVMVGGDKAIFDKYYDLMKAMA 156
Cdd:PRK09599 78 DELAPLLSPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGG----VWGLErgyCLMIGGDKEAVERLEPIFKALA 153
|
170 180
....*....|....*....|
gi 162139755 157 ----GSVVHTGEIGAGNVTK 172
Cdd:PRK09599 154 praeDGYLHAGPVGAGHFVK 173
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-99 |
5.48e-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: 55.84 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYS---LVVADRNPEAIADVIAA-GAETASTAKAIAEQCDVII-TMLPNspHVKEV 75
Cdd:COG0345 1 MSMKIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERyGVRVTTDNAEAAAQADVVVlAVKPQ--DLAEV 78
|
90 100
....*....|....*....|....
gi 162139755 76 AlgeNGIIEGAKPGTVLIdmsSIA 99
Cdd:COG0345 79 L---EELAPLLDPDKLVI---SIA 96
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-63 |
3.84e-08 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 53.23 E-value: 3.84e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYS---LVVADRNPEAIADVIAA-GAETASTAKAIAEQCDVII 63
Cdd:PRK11880 1 MMKKIGFIGGGNMASAIIGGLLASGVPakdIIVSDPSPEKRAALAEEyGVRAATDNQEAAQEADVVV 67
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
3-264 |
2.10e-06 |
|
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: 48.76 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNP-------------------EAIADVIAAGAETAST-AKAIAEQCDVI 62
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQekvdklnkgkspiyepgldELLAKALKAGRLRATTdYEEAIRDADVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 63 ITMLP------NSP---HVKEVAlgeNGIIEGAKPGTVLIDMSSIAP-----LASREISEALKAKG--IDMLDAPVSGGE 126
Cdd:TIGR03026 81 IICVPtplkedGSPdlsYVESAA---ETIAKHLRKGATVVLESTVPPgtteeVVKPILERSGLKLGedFYLAYNPEFLRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 127 PKAIDGTLS---VMVGGDKAIFDKYYDLMKAMAGSVVHTGEIGAGNVTKLANQVIVALNIAAMSEALTLATKAGVNpdlV 203
Cdd:TIGR03026 158 GNAVHDLLHpdrIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALGID---V 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 162139755 204 YQAIRGGlagstvldAKAPMVMDRNFKPGFRIDLHI--KDLANALDTSHGVGAQLPLTAAVME 264
Cdd:TIGR03026 235 YEVIEAA--------GTDPRIGFNFLNPGPGVGGHCipKDPLALIAKAKELGYNPELIEAARE 289
|
|
| COG2085 |
COG2085 |
Predicted dinucleotide-binding enzyme [General function prediction only]; |
5-94 |
2.84e-06 |
|
Predicted dinucleotide-binding enzyme [General function prediction only];
Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 47.09 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 5 VGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIA---AGAETASTAKAiAEQCDVIITMLPNSpHVKEVAlgenG 81
Cdd:COG2085 1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEKAAALAAelgPGARAGTNAEA-AAAADVVVLAVPYE-AVPDVL----E 74
|
90
....*....|...
gi 162139755 82 IIEGAKPGTVLID 94
Cdd:COG2085 75 SLGDALAGKIVID 87
|
|
| PTZ00142 |
PTZ00142 |
6-phosphogluconate dehydrogenase; Provisional |
5-192 |
7.93e-06 |
|
6-phosphogluconate dehydrogenase; Provisional
Pssm-ID: 240287 [Multi-domain] Cd Length: 470 Bit Score: 47.09 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 5 VGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIA---------AGAETASTAKAIAEQCDVIITMLPNSPHVKEV 75
Cdd:PTZ00142 4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFVKkakegntrvKGYHTLEELVNSLKKPRKVILLIKAGEAVDET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 76 AlgeNGIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLMKAM 155
Cdd:PTZ00142 84 I---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKC 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 162139755 156 AGSV------VHTGEIGAGNVTKLANQVIVALNIAAMSEALTL 192
Cdd:PTZ00142 160 SAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISESYKL 202
|
|
| PLN02350 |
PLN02350 |
phosphogluconate dehydrogenase (decarboxylating) |
4-173 |
1.37e-05 |
|
phosphogluconate dehydrogenase (decarboxylating)
Pssm-ID: 215200 [Multi-domain] Cd Length: 493 Bit Score: 46.25 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIA-AGAE----------TASTAKAIAEQCDVIITMLPNSPhv 72
Cdd:PLN02350 8 RIGLAGLAVMGQNLALNIAEKGFPISVYNRTTSKVDETVErAKKEgnlplygfkdPEDFVLSIQKPRSVIILVKAGAP-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 73 keVALGENGIIEGAKPGTVLIDMSSIAPLASREISEALKAKGIDMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLM 152
Cdd:PLN02350 86 --VDQTIKALSEYMEPGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNIEDIL 162
|
170 180
....*....|....*....|....*..
gi 162139755 153 KAMAGS------VVHTGEIGAGNVTKL 173
Cdd:PLN02350 163 EKVAAQvddgpcVTYIGPGGAGNFVKM 189
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
3-98 |
1.66e-05 |
|
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: 45.50 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVA--DRNPEAIADVIAAGA--ETASTAKAIAEQCDVIITMLPnsphVKEVA-- 76
Cdd:COG0287 2 MRIAIIGLGLIGGSLALALKRAGLAHEVVgvDRSPETLERALELGVidRAATDLEEAVADADLVVLAVP----VGATIev 77
|
90 100
....*....|....*....|..
gi 162139755 77 LGEngIIEGAKPGTVLIDMSSI 98
Cdd:COG0287 78 LAE--LAPHLKPGAIVTDVGSV 97
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
19-115 |
5.06e-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: 42.41 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 19 KNLLKAGYSLVVADRNPEAI----ADVIAAGAETASTAKAIAEQCDVIItmlpnspHVKEVALGEngiIEGAKPGTVLID 94
Cdd:pfam05222 21 KKLVKLGHEVLVESGAGLGAgfsdEAYEAAGAEIVDTAAEVWAEADLIL-------KVKEPQPEE---YALLREGQTLIT 90
|
90 100
....*....|....*....|.
gi 162139755 95 MssIAPLASREISEALKAKGI 115
Cdd:pfam05222 91 F--LHPAANPELLEALAAKGV 109
|
|
| PRK08655 |
PRK08655 |
prephenate dehydrogenase; Provisional |
3-162 |
8.29e-05 |
|
prephenate dehydrogenase; Provisional
Pssm-ID: 236326 [Multi-domain] Cd Length: 437 Bit Score: 43.82 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIG-LGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAA-GAETASTAKAIAEQCDVIITMLP---NSPHVKEVAl 77
Cdd:PRK08655 1 MKISIIGgTGGLGKWFARFLKEKGFEVIVTGRDPKKGKEVAKElGVEYANDNIDAAKDADIVIISVPinvTEDVIKEVA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 78 gengiiEGAKPGTVLIDMSSIAPLASREISEALKaKGIDMLDA-PVSGGEPKAIDGTLSVMV---GGDKAIFDKYYDLMK 153
Cdd:PRK08655 80 ------PHVKEGSLLMDVTSVKERPVEAMEEYAP-EGVEILPThPMFGPRTPSLKGQVVILTpteKRSNPWFDKVKNFLE 152
|
....*....
gi 162139755 154 AMAGSVVHT 162
Cdd:PRK08655 153 KEGARVIVT 161
|
|
| F420_oxidored |
pfam03807 |
NADP oxidoreductase coenzyme F420-dependent; |
6-96 |
2.22e-04 |
|
NADP oxidoreductase coenzyme F420-dependent;
Pssm-ID: 397743 [Multi-domain] Cd Length: 92 Bit Score: 39.52 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 6 GFIGLGIMGKPMSKNLLKAGYS--LVVADRNPE---AIADVIAAGAETASTAKAiAEQCDVIITMLPnsPHVKEVALGEn 80
Cdd:pfam03807 1 GFIGAGNMGEALARGLVAAGPHevVVANSRNPEkaeELAEEYGVGATAVDNEEA-AEEADVVFLAVK--PEDAPDVLSE- 76
|
90
....*....|....*.
gi 162139755 81 giIEGAKPGTVLIDMS 96
Cdd:pfam03807 77 --LSDLLKGKIVISIA 90
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-77 |
2.95e-04 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 41.83 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLK-AGYSLV-VADRNPEAIADVIAA-GAETASTAKAIAEQCD---VIITmLPNSPHVkE 74
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAAlPGVELVaVADRDPERAEAFAEEyGVRVYTDYEELLADPDidaVVIA-TPNHLHA-E 79
|
...
gi 162139755 75 VAL 77
Cdd:COG0673 80 LAI 82
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
19-115 |
3.65e-04 |
|
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: 39.71 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 19 KNLLKAGYSLVVADRNPEAI----ADVIAAGAETASTAKAIAeQCDVIItmlpnspHVKEVALGEngiIEGAKPGTVLID 94
Cdd:smart01003 21 KKLVKLGHEVLVESGAGEGAgfsdEAYEAAGAEIVDTAEVWA-DADIIL-------KVKEPSPEE---LALLREGQILFG 89
|
90 100
....*....|....*....|.
gi 162139755 95 MssIAPLASREISEALKAKGI 115
Cdd:smart01003 90 Y--LHPAANPELLEALAAKGV 108
|
|
| COG5495 |
COG5495 |
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ... |
1-63 |
4.00e-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: 41.34 E-value: 4.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162139755 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLV-VADRNPEAiADVIAA--GAETASTAKAIAEQCDVII 63
Cdd:COG5495 2 ARMKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPAS-AERAAAllGAVPALDLEELAAEADLVL 66
|
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| PRK09287 |
PRK09287 |
NADP-dependent phosphogluconate dehydrogenase; |
13-168 |
1.59e-03 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236453 [Multi-domain] Cd Length: 459 Bit Score: 39.72 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 13 MGKPMSKNLLKAGYSLVVADRNPEAIADVIAA--------GAETASTAKAIAEQCDVIITMLPNSPHVKEValgengiIE 84
Cdd:PRK09287 1 MGKNLALNIASHGYTVAVYNRTPEKTDEFLAEegkgkkivPAYTLEEFVASLEKPRKILLMVKAGAPVDAV-------IE 73
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 85 GAKP----GTVLID------MSSIAplasREisEALKAKGIDMLDAPVSGGEPKAIDGTlSVMVGGDKAIFDKYYDLMKA 154
Cdd:PRK09287 74 QLLPllekGDIIIDggnsnyKDTIR----RE--KELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGQKEAYELVAPILEK 146
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170 180
....*....|....*....|.
gi 162139755 155 MAGSVV-------HTGEIGAG 168
Cdd:PRK09287 147 IAAKVEdgepcvtYIGPDGAG 167
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| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
37-179 |
1.71e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 39.31 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 37 AIADVIAAGAETASTAKAIAEQCDVIITMlpNSPHVKEVALgengiiegAKPGTVLIDMSSIAplASREISEALKAKGI- 115
Cdd:cd01620 45 SDEDYLQAGAQIVPAASKEAYSADIIVKL--KEPEFAEYDL--------IKKGQLLVTFLHAA--TNRGVVEVLMRKKLt 112
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 116 --DMLDAPVSGGEPKAIDGTLSvmvgGDKAIFDKYYDLMKAMAGSVVHTGE--------IGAGNV--------TKLANQV 177
Cdd:cd01620 113 ayALEDLENDFRPRLAPNSNIA----GYAGVQLGAYELARIQGGRMGGAGGvppakvliIGAGVVglgaakiaKKLGANV 188
|
..
gi 162139755 178 IV 179
Cdd:cd01620 189 LV 190
|
|
| NAD_bind_Leu_Phe_Val_DH |
cd01075 |
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
3-61 |
8.33e-03 |
|
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133444 Cd Length: 200 Bit Score: 36.80 E-value: 8.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162139755 3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVADRNPEAIADVIAA-GAETASTAKAIAEQCDV 61
Cdd:cd01075 29 KTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELfGATVVAPEEIYSVDADV 88
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