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Conserved domains on  [gi|15829824|ref|NP_308597|]
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tartronate semialdehyde reductase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

2-hydroxy-3-oxopropionate reductase( domain architecture ID 11487600)

2-hydroxy-3-oxopropionate reductase catalyzes the reduction of tatronate semialdehyde to D-glycerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-292 0e+00

2-hydroxy-3-oxopropionate reductase;


:

Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 574.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240
Cdd:PRK15059 161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829824  241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
Cdd:PRK15059 241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
 
Name Accession Description Interval E-value
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-292 0e+00

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 574.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240
Cdd:PRK15059 161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829824  241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
Cdd:PRK15059 241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-291 0e+00

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: 509.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPeVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15829824   241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKL 291
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-283 2.13e-124

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 356.35  E-value: 2.13e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGC 79
Cdd:COG2084   2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPaKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
Cdd:COG2084  82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15829824 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
Cdd:COG2084 242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-160 3.60e-61

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 191.14  E-value: 3.60e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPeKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    81 KASlKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:pfam03446  81 GLK-PGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
 
Name Accession Description Interval E-value
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
1-292 0e+00

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 574.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:PRK15059   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240
Cdd:PRK15059 161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829824  241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
Cdd:PRK15059 241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
tartro_sem_red TIGR01505
2-hydroxy-3-oxopropionate reductase; This model represents 2-hydroxy-3-oxopropionate reductase ...
 2-291 0e+00

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: 509.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:TIGR01505   1 KVGFIGLGIMGSPMSINLAKAGYQLHVTTIGPeVADELLAAGAVTAETARQVTEQADVIFTMVPDSPQVEEVAFGENGII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:TIGR01505  81 EGAKPGKTLVDMSSISPIESKRFAKAVKEKGIDYLDAPVSGGEIGAIEGTLSIMVGGDQAVFDRVKPLFEALGKNIVLVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   161 GNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDLN 240
Cdd:TIGR01505 161 GNGDGQTCKVANQIIVALNIEAVSEALVFASKAGVDPVRVRQALRGGLAGSTVLEVKGERVIDRTFKPGFRIDLHQKDLN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15829824   241 LALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKL 291
Cdd:TIGR01505 241 LALDSAKAVGANLPNTATVQELFNTLRANGGGQLDHSALVQALELLANHKV 291
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 1-283 2.13e-124

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 356.35  E-value: 2.13e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGC 79
Cdd:COG2084   2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPaKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
Cdd:COG2084  82 LAALRPGAVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVHV 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239
Cdd:COG2084 162 GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLKDL 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15829824 240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
Cdd:COG2084 242 GLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
garR PRK11559
tartronate semialdehyde reductase; Provisional
 1-288 6.07e-111

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 322.77  E-value: 6.07e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGC 79
Cdd:PRK11559   3 MKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAvAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   80 TKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLV 159
Cdd:PRK11559  83 IEGAKPGTVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSVVHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQKDL 239
Cdd:PRK11559 163 GDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIKDL 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15829824  240 NLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMAN 288
Cdd:PRK11559 243 ANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAK 291
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 2-160 3.60e-61

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 191.14  E-value: 3.60e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPeKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFGEGLLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    81 KASlKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:pfam03446  81 GLK-PGDIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTYIG 159
HIBADH TIGR01692
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ...
 5-283 9.56e-57

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: 184.23  E-value: 9.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     5 FIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCTKAS 83
Cdd:TIGR01692   1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAvEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    84 LKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVGGNG 163
Cdd:TIGR01692  81 AKGSLLIDCSTIDPDSARKLAELAAAHGAVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNIVHCGDHG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   164 DGQTCKVANQIIVALNIEAVSEALLFASKAGADPVR----VRQALMGGFASSRILEVHG---ERMIKRTFNPGFKIALHQ 236
Cdd:TIGR01692 161 AGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVlfeiANTSSGRCWSSDTYNPVPGvmpQAPASNGYQGGFGTALML 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 15829824   237 KDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
Cdd:TIGR01692 241 KDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
 163-283 5.89e-46

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: 150.75  E-value: 5.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   163 GDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILE-VHGERMIKRTFNPGFKIALHQKDLNL 241
Cdd:pfam14833   1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALEnKFPQRVLSRDFDPGFALDLMLKDLGL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 15829824   242 ALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQAL 283
Cdd:pfam14833  81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
2-287 2.66e-40

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 141.92  E-value: 2.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:PRK15461   3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAvDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITLVG 160
Cdd:PRK15461  83 EGLSRDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELINAG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  161 GNGDGQTCKVANQII-VALNieAVS-EALLFASKAGAdPVRVRQALMGGFASSR--ILEVHGERMIKRTFNPGFKIALHQ 236
Cdd:PRK15461 163 GPGMGIRVKLINNYMsIALN--ALSaEAAVLCEALGL-SFDVALKVMSGTAAGKghFTTTWPNKVLKGDLSPAFMIDLAH 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15829824  237 KDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMA 287
Cdd:PRK15461 240 KDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSA 290
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-292 6.07e-33

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 128.05  E-value: 6.07e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARA-----GHQLHVTTIGPVADellsLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGE 76
Cdd:PLN02858  326 RIGFIGLGAMGFGMASHLLKSnfsvcGYDVYKPTLVRFEN----AGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGD 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    77 NGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGD--YLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGK 154
Cdd:PLN02858  402 LGAVSALPAGASIVLSSTVSPGFVIQLERRLENEGRDikLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSE 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   155 NITLV-GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIA 233
Cdd:PLN02858  482 KLYVIkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALD 561

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829824   234 LHQKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKLA 292
Cdd:PLN02858  562 IFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVE 620
PLN02858 PLN02858
fructose-bisphosphate aldolase
 2-274 1.70e-30

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 120.73  E-value: 1.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     2 KLGFIGLGIMGTPMAINLARAGHQLHVTTIG-PVADELLSLGAVNVDTARQVTEAADIIFIMVPDTPQVEEVLFGENGCT 80
Cdd:PLN02858    6 VVGFVGLDSLSFELASSLLRSGFKVQAFEIStPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDEGAA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    81 KASLKGKTIVDMSSISPIETKRFARQVNELGGD--YLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITL 158
Cdd:PLN02858   86 KGLQKGAVILIRSTILPLQLQKLEKKLTERKEQifLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQKLYT 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   159 V-GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQK 237
Cdd:PLN02858  166 FeGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDYIEGRFLNVLVQ 245

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 15829824   238 DLNLALQSAKALALNLPNTATC-QELFNTCAANGGSQL 274
Cdd:PLN02858  246 NLGIVLDMAKSLPFPLPLLAVAhQQLISGSSSMQGDDT 283
YqeC COG1023
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
1-152 1.38e-22

6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];


Pssm-ID: 440646 [Multi-domain]  Cd Length: 300  Bit Score: 94.77  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAAD---IIFIMVPDTPQVEEVLfge 76
Cdd:COG1023   1 MQIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPeAVAALAAEGATGADSLEELVAKLPaprVVWLMVPAGEITDQVI--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  77 ngctkASL-----KGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGtLSIMVGGDEAVFERVKPLFEL 151
Cdd:COG1023  78 -----EELapllePGDIVIDGGNSNYKDDIRRAEELAEKGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVERLEPIFKA 151


                .
gi 15829824 152 L 152
Cdd:COG1023 152 L 152
PRK09599 PRK09599
NADP-dependent phosphogluconate dehydrogenase;
1-152 5.12e-22

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236582 [Multi-domain]  Cd Length: 301  Bit Score: 93.27  E-value: 5.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVNVDTARQVTEAAD---IIFIMVPDTPQVEEVLfge 76
Cdd:PRK09599   1 MQLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPeAVEALAEEGATGADSLEELVAKLPaprVVWLMVPAGEITDATI--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   77 ngctkASL-----KGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGtLSIMVGGDEAVFERVKPLFEL 151
Cdd:PRK09599  78 -----DELapllsPGDIVIDGGNSYYKDDIRRAELLAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIFKA 151


                 .
gi 15829824  152 L 152
Cdd:PRK09599 152 L 152
gnd_rel TIGR00872
6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) ...
 1-196 7.78e-18

6-phosphogluconate dehydrogenase (decarboxylating); This family resembles a larger family (gnd) of bacterial and eukaryotic 6-phosphogluconate dehydrogenases but differs from it by a deep split in a UPGMA similarity clustering tree and the lack of a central region of about 140 residues. Among complete genomes, it is found is found in Bacillus subtilis and Mycobacterium tuberculosis, both of which also contain gnd, and in Aquifex aeolicus. The protein from Methylobacillus flagellatus KT has been characterized as a decarboxylating 6-phosphogluconate dehydrogenase as part of an unusual formaldehyde oxidation cycle. In some sequenced organisms members of this family are the sole 6-phosphogluconate dehydrogenase present and are probably active in the pentose phosphate cycle. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273313 [Multi-domain]  Cd Length: 298  Bit Score: 81.82  E-value: 7.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGPVA-DELLSLGAVNVDTARQVTE---AADIIFIMVPDTPqVEEVLfgE 76
Cdd:TIGR00872   1 MQLGLIGLGRMGANIVRRLAKRGHDCVGYDHDQDAvKAMKEDRTTGVANLRELSQrlsAPRVVWVMVPHGI-VDAVL--E 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    77 NGCTKASlKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGtLSIMVGGDEAVFERVKPLFELLG--- 153
Cdd:TIGR00872  78 ELAPTLE-KGDIVIDGGNSYYKDSLRRYKLLKEKGIHLLDCGTSGGVWGRERG-YCFMIGGDGEAFARAEPLFADVApee 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15829824   154 KNITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGAD 196
Cdd:TIGR00872 156 QGYLYCGPCGSGHFVKMVHNGIEYGMMAAIAEGFEILRNSQFD 198
Gnd COG0362
6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate ...
 4-150 1.14e-12

6-phosphogluconate dehydrogenase [Carbohydrate transport and metabolism]; 6-phosphogluconate dehydrogenase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440131 [Multi-domain]  Cd Length: 467  Bit Score: 67.79  E-value: 1.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   4 GFIGLGIMGTPMAINLARAGHQLHV---TTigPVADELLSlgavNVDTARQVTEAADI------------IFIMVPDTPQ 68
Cdd:COG0362   6 GVIGLAVMGRNLALNIADHGFSVAVynrTA--EKTDAFLA----EHGKGKNIVGTYSLeefvaslerprkILLMVKAGKP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824  69 VEEVLfgengctkASL-----KGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTlSIMVGGDEAVFE 143
Cdd:COG0362  80 VDAVI--------EQLlpllePGDIIIDGGNSHFTDTIRREKELAEKGIHFIGMGVSGGEEGALHGP-SIMPGGSKEAYE 150


                ....*..
gi 15829824 144 RVKPLFE 150
Cdd:COG0362 151 LVKPILE 157
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
 3-186 4.64e-08

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 53.64  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    3 LGFIGLGIMGTPMAINLARAGHQLHV---------TTIGPVADELLSL-GAVNVDTARQVTEAADIIFIMVPDTPQVEEV 72
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVynrtyekteEFVKKAKEGNTRVkGYHTLEELVNSLKKPRKVILLIKAGEAVDET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   73 LfgeNGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTlSIMVGGDEAVFERVKPLFELL 152
Cdd:PTZ00142  84 I---DNLLPLLEKGDIIIDGGNEWYLNTERRIKRCEEKGILYLGMGVSGGEEGARYGP-SLMPGGNKEAYDHVKDILEKC 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15829824  153 GKNI------TLVGGNGDGQTCKVANQIIVALNIEAVSEA 186
Cdd:PTZ00142 160 SAKVgdspcvTYVGPGSSGHYVKMVHNGIEYGDMQLISES 199
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 1-254 1.20e-07

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: 52.23  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824     1 MKLGFIGLGIMGTPMAINLARAGHqlHVT------------------TIGPVADELLSlGAVNVDTARQVTEA------A 56
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGH--DVTgvdidqekvdklnkgkspIYEPGLDELLA-KALKAGRLRATTDYeeairdA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    57 DIIFIMVP---------DTPQVEEVLfgeNGCTKASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVsggEIG-- 125
Cdd:TIGR03026  78 DVIIICVPtplkedgspDLSYVESAA---ETIAKHLRKGATVVLESTVPPGTTEEVVKPILERSGLKLGEDF---YLAyn 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   126 ---AREGTL--------SIMVGGDEAVFERVKPLFELLGKNITLVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAG 194
Cdd:TIGR03026 152 pefLREGNAvhdllhpdRIVGGETEEAGEAVAELYSPIIDGPVLVTSIETAEMIKLAENTFRAVKIAFANELARICEALG 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829824   195 ADPVRVRQAlMGgfassrilevHGERMIKRTFNPGFKIALH--QKDLNLALQSAKALALNLP 254
Cdd:TIGR03026 232 IDVYEVIEA-AG----------TDPRIGFNFLNPGPGVGGHciPKDPLALIAKAKELGYNPE 282
PRK09287 PRK09287
NADP-dependent phosphogluconate dehydrogenase;
119-150 2.16e-07

NADP-dependent phosphogluconate dehydrogenase;


Pssm-ID: 236453 [Multi-domain]  Cd Length: 459  Bit Score: 51.66  E-value: 2.16e-07
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15829824  119 VSGGEIGAREGTlSIMVGGDEAVFERVKPLFE 150
Cdd:PRK09287 115 VSGGEEGALHGP-SIMPGGQKEAYELVAPILE 145
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 1-72 1.13e-05

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 45.96  E-value: 1.13e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAGHQLH-VTTIGPVADELLS--LGAVNVDTARQVTEAADIIFIMVPDTpQVEEV 72
Cdd:COG5495   4 MKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAalLGAVPALDLEELAAEADLVLLAVPDD-AIAEV 77
PLN02350 PLN02350
phosphogluconate dehydrogenase (decarboxylating)
 2-186 3.02e-05

phosphogluconate dehydrogenase (decarboxylating)


Pssm-ID: 215200 [Multi-domain]  Cd Length: 493  Bit Score: 45.09  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824    2 KLGFIGLGIMGTPMAINLARAGHQLHV---------TTIGPVADE--LLSLGAVNVDTARQVTEAADIIFIMVPDTPQVE 70
Cdd:PLN02350   8 RIGLAGLAVMGQNLALNIAEKGFPISVynrttskvdETVERAKKEgnLPLYGFKDPEDFVLSIQKPRSVIILVKAGAPVD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   71 EvlfgengcTKASL-----KGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTlSIMVGGDEAVFERV 145
Cdd:PLN02350  88 Q--------TIKALseymePGDCIIDGGNEWYENTERRIKEAAEKGLLYLGMGVSGGEEGARNGP-SLMPGGSFEAYKNI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15829824  146 KPLFELL------GKNITLVGGNGDGQTCKVANQIIVALNIEAVSEA 186
Cdd:PLN02350 159 EDILEKVaaqvddGPCVTYIGPGGAGNFVKMVHNGIEYGDMQLISEA 205
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-113 5.94e-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: 43.58  E-value: 5.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAGHQLHVTTIGP---VADELLSLGAVN--VDTARQVTEAADIIFIMVPdTPQVEEVLfG 75
Cdd:COG0287   2 MRIAIIGLGLIGGSLALALKRAGLAHEVVGVDRspeTLERALELGVIDraATDLEEAVADADLVVLAVP-VGATIEVL-A 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15829824  76 ENgctKASLKGKTIV-DMSSispieTKR-FARQVNELGGD 113
Cdd:COG0287  80 EL---APHLKPGAIVtDVGS-----VKGaVVEAAEALLPD 111
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-73 3.31e-04

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: 41.20  E-value: 3.31e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829824   1 MKLGFIGLGIMGTPMAINLARAG---HQLHVTTIGPVADELLS--LGAVNVDTARQVTEAADIIFIMVPdtPQ-VEEVL 73
Cdd:COG0345   3 MKIGFIGAGNMGSAIIKGLLKSGvppEDIIVSDRSPERLEALAerYGVRVTTDNAEAAAQADVVVLAVK--PQdLAEVL 79
PRK11880 PRK11880
pyrroline-5-carboxylate reductase; Reviewed
 1-73 1.49e-03

pyrroline-5-carboxylate reductase; Reviewed


Pssm-ID: 237008 [Multi-domain]  Cd Length: 267  Bit Score: 39.36  E-value: 1.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAG---HQLHVTTIGP-VADELLS-LGAVNVDTARQVTEAADIIFIMVpdTPQV-EEVL 73
Cdd:PRK11880   3 KKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPeKRAALAEeYGVRAATDNQEAAQEADVVVLAV--KPQVmEEVL 79
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 5-73 1.79e-03

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 39.50  E-value: 1.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829824    5 FIGLGIMGTPMAINLARAGHQLHVTTIGPVADEL---LSLGAVN--VDTARQVTEAADIIFIMVPdTPQVEEVL 73
Cdd:PRK06545   5 IVGLGLIGGSLALAIKAAGPDVFIIGYDPSAAQLaraLGFGVIDelAADLQRAAAEADLIVLAVP-VDATAALL 77
PLN02688 PLN02688
pyrroline-5-carboxylate reductase
 1-69 5.71e-03

pyrroline-5-carboxylate reductase


Pssm-ID: 178291 [Multi-domain]  Cd Length: 266  Bit Score: 37.63  E-value: 5.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829824    1 MKLGFIGLGIMGTPMAINLARAG----HQLHVTTIGPVADELL--SLGAVNVDTARQVTEAADIIFIMVpdTPQV 69
Cdd:PLN02688   1 FRVGFIGAGKMAEAIARGLVASGvvppSRISTADDSNPARRDVfqSLGVKTAASNTEVVKSSDVIILAV--KPQV 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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