|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
1-212 |
2.36e-133 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 373.04 E-value: 2.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 1 MNHWNTSAESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQL 80
Cdd:PRK05718 1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 81 AQVTEAGAQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCP 160
Cdd:PRK05718 81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490366259 161 TGGISPENYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVAGAQ 212
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
8-211 |
2.73e-101 |
|
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]
Pssm-ID: 273490 Cd Length: 204 Bit Score: 291.52 E-value: 2.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 8 AESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAG 87
Cdd:TIGR01182 1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 88 AQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPE 167
Cdd:TIGR01182 81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490366259 168 NYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVAGA 211
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
9-203 |
7.37e-101 |
|
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate aldolase (KHG-aldolase) Phospho-2-dehydro-3-deoxygluconate aldolase (KDPG-aldolase)
Pssm-ID: 395858 Cd Length: 196 Bit Score: 290.14 E-value: 7.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 9 ESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGA 88
Cdd:pfam01081 2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 89 QFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPEN 168
Cdd:pfam01081 82 QFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPAN 161
|
170 180 190
....*....|....*....|....*....|....*
gi 490366259 169 YRNYLALESVLCIGGSWLVPSDAVKAGDYQRITEL 203
Cdd:pfam01081 162 VRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
4-209 |
3.44e-91 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 266.18 E-value: 3.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 4 WNTSAESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEV-PEAIVGAGTVINPQQLAQ 82
Cdd:COG0800 1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 83 VTEAGAQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEAnGGVKALKAIAGPFSQVRFCPTG 162
Cdd:COG0800 81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490366259 163 GISPENYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVA 209
Cdd:COG0800 160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
12-203 |
2.25e-79 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 235.49 E-value: 2.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 12 LKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGAQFA 91
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 92 ISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANgGVKALKAIAGPFSQVRFCPTGGISPENYRN 171
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159
|
170 180 190
....*....|....*....|....*....|..
gi 490366259 172 YLALeSVLCIGGSWLVPSDAVKAGDYQRITEL 203
Cdd:cd00452 160 WLAA-GVVAVGGGSLLPKDAVAAGDWAAITAL 190
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
1-212 |
2.36e-133 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 373.04 E-value: 2.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 1 MNHWNTSAESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQL 80
Cdd:PRK05718 1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 81 AQVTEAGAQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCP 160
Cdd:PRK05718 81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490366259 161 TGGISPENYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVAGAQ 212
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
8-211 |
2.73e-101 |
|
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an enzyme of the Entner-Doudoroff pathway. This aldolase has another function, 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) shown experimentally in Escherichia coli and Pseudomonas putida [Amino acid biosynthesis, Glutamate family, Energy metabolism, Entner-Doudoroff]
Pssm-ID: 273490 Cd Length: 204 Bit Score: 291.52 E-value: 2.73e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 8 AESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAG 87
Cdd:TIGR01182 1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 88 AQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPE 167
Cdd:TIGR01182 81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490366259 168 NYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVAGA 211
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
9-203 |
7.37e-101 |
|
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate aldolase (KHG-aldolase) Phospho-2-dehydro-3-deoxygluconate aldolase (KDPG-aldolase)
Pssm-ID: 395858 Cd Length: 196 Bit Score: 290.14 E-value: 7.37e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 9 ESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGA 88
Cdd:pfam01081 2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 89 QFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPEN 168
Cdd:pfam01081 82 QFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPAN 161
|
170 180 190
....*....|....*....|....*....|....*
gi 490366259 169 YRNYLALESVLCIGGSWLVPSDAVKAGDYQRITEL 203
Cdd:pfam01081 162 VRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
4-209 |
3.44e-91 |
|
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; 2-keto-3-deoxy-6-phosphogluconate aldolase is part of the Pathway/BioSystem: Entner-Doudoroff pathway
Pssm-ID: 440563 Cd Length: 213 Bit Score: 266.18 E-value: 3.44e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 4 WNTSAESVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEV-PEAIVGAGTVINPQQLAQ 82
Cdd:COG0800 1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 83 VTEAGAQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEAnGGVKALKAIAGPFSQVRFCPTG 162
Cdd:COG0800 81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490366259 163 GISPENYRNYLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVA 209
Cdd:COG0800 160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
12-203 |
2.25e-79 |
|
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.
Pssm-ID: 188632 Cd Length: 190 Bit Score: 235.49 E-value: 2.25e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 12 LKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGAQFA 91
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 92 ISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANgGVKALKAIAGPFSQVRFCPTGGISPENYRN 171
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159
|
170 180 190
....*....|....*....|....*....|..
gi 490366259 172 YLALeSVLCIGGSWLVPSDAVKAGDYQRITEL 203
Cdd:cd00452 160 WLAA-GVVAVGGGSLLPKDAVAAGDWAAITAL 190
|
|
| PRK06015 |
PRK06015 |
2-dehydro-3-deoxy-phosphogluconate aldolase; |
12-209 |
6.10e-74 |
|
2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 168348 Cd Length: 201 Bit Score: 222.00 E-value: 6.10e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 12 LKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGAQFA 91
Cdd:PRK06015 1 LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 92 ISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPENYRN 171
Cdd:PRK06015 81 VSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 490366259 172 YLALESVLCIGGSWLVPSDAVKAGDYQRITELAKEAVA 209
Cdd:PRK06015 161 YLSLPNVVCVGGSWVAPKELVAAGDWAGITKLAAEAAA 198
|
|
| PRK07455 |
PRK07455 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
10-173 |
1.10e-33 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 180985 Cd Length: 187 Bit Score: 118.99 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 10 SVLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGAQ 89
Cdd:PRK07455 7 AQLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 90 FAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANGGVKALKAIAGPFSQVRFCPTGGISPENY 169
Cdd:PRK07455 87 FCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENA 166
|
....
gi 490366259 170 RNYL 173
Cdd:PRK07455 167 QAFI 170
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
12-209 |
1.32e-33 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 119.33 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 12 LKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIA---KEVPEAIVGAGTVINPQQLAQVTEAGA 88
Cdd:PRK06552 10 LKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVelyKDDPEVLIGAGTVLDAVTARLAILAGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 89 QFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANgGVKALKAIAGPFSQVRFCPTGGISPEN 168
Cdd:PRK06552 90 QFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTL-GPSFIKAIKGPLPQVNVMVTGGVNLDN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490366259 169 YRNYLAL-ESVLCIGGSWLVPSdavKAGDYQRITELAKEAVA 209
Cdd:PRK06552 169 VKDWFAAgADAVGIGGELNKLA---SQGDFDLITEKAKKYMS 207
|
|
| PRK07114 |
PRK07114 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
11-209 |
1.98e-30 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 235939 Cd Length: 222 Bit Score: 111.65 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 11 VLKSGPVVPVIVINHIEEAVPVAKALVAGGVKVLEVTLRTDCAIEA----IRRIAKEVPEAIVGAGTVINPQQLAQVTEA 86
Cdd:PRK07114 11 AMKATGMVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVfaelVKYAAKELPGMILGVGSIVDAATAALYIQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 87 GAQFAISPGLTDALLKAAVAGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEAnGGVKALKAIAGPFSQVRFCPTGGISP 166
Cdd:PRK07114 91 GANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGSV-YGPGFVKAIKGPMPWTKIMPTGGVEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490366259 167 --ENYRNYLAlESVLCIG-GSWLVPSDAVKAGDYQRITELAKEAVA 209
Cdd:PRK07114 170 teENLKKWFG-AGVTCVGmGSKLIPKEALAAKDYAGIEQKVREALA 214
|
|
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
27-174 |
9.70e-26 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 98.75 E-value: 9.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490366259 27 EEAVPVAKALVAGGVKVLEVTLRTDCAIEAIRRIAKEVP-EAIVGAGTVINPQQLAQVTEAGAQFAISPGLTDALLKAAV 105
Cdd:PRK09140 22 DEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGdRALIGAGTVLSPEQVDRLADAGGRLIVTPNTDPEVIRRAV 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490366259 106 AGSIPLIPGISTVSELMLGMSYGLNEFKFFPAEANG--GVKALKAIAGPfsQVRFCPTGGISPENYRNYLA 174
Cdd:PRK09140 102 ALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVLPP--DVPVFAVGGVTPENLAPYLA 170
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|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
33-88 |
5.54e-03 |
|
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.
Pssm-ID: 238223 [Multi-domain] Cd Length: 325 Bit Score: 37.11 E-value: 5.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490366259 33 AKALVAGGVKVLEVtlrtDCA-------IEAIRRIAKEVPEAIVGAGTVINPQQLAQVTEAGA 88
Cdd:cd00381 99 AEALVEAGVDVIVI----DSAhghsvyvIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGA 157
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|
| DUF6506 |
pfam20116 |
Family of unknown function (DUF6506); This family of proteins is functionally uncharacterized. ... |
20-71 |
6.18e-03 |
|
Family of unknown function (DUF6506); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are approximately 100 amino acids in length.
Pssm-ID: 437948 Cd Length: 96 Bit Score: 34.78 E-value: 6.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 490366259 20 VIVINHIEEAVPVAKALVAGGVKVLEVtlrtdCA---IEAIRRIAKEVPEAI-VGA 71
Cdd:pfam20116 30 VVGVKDYEEAVEVAKELVEEGVQAIEL-----CGgfgPEGAARIIEAVGGKVpVGV 80
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