|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
11-217 |
1.22e-99 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 287.91 E-value: 1.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 11 YHRERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQ 90
Cdd:PRK05718 3 NWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 91 VEAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTG 170
Cdd:PRK05718 83 AIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1862651764 171 GIRRNTAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:PRK05718 163 GISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVA 209
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
16-217 |
6.33e-89 |
|
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: 260.32 E-value: 6.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 16 VRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAG 95
Cdd:TIGR01182 1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 96 AQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRN 175
Cdd:TIGR01182 81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1862651764 176 TAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALE 202
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
13-217 |
3.17e-83 |
|
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: 246.15 E-value: 3.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 13 RERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKA-IPDAWVGAGTVTSIAQYRQV 91
Cdd:COG0800 2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEvGPDALVGAGTVLTPEQARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 92 EAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAgGIPALKAFSGPFPDVTFCPTGG 171
Cdd:COG0800 82 IAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1862651764 172 IRRNTAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:COG0800 161 VSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
16-211 |
3.55e-83 |
|
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: 245.46 E-value: 3.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 16 VRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAG 95
Cdd:pfam01081 1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 96 AQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRN 175
Cdd:pfam01081 81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1862651764 176 TAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEI 211
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
20-211 |
1.50e-70 |
|
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: 213.15 E-value: 1.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 20 LQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAGAQFV 99
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 100 ITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAgGIPALKAFSGPFPDVTFCPTGGIRRNTAAD 179
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159
|
170 180 190
....*....|....*....|....*....|..
gi 1862651764 180 YLALGnVQAVGGTWLTPADVVAAKDWSQITEI 211
Cdd:cd00452 160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05718 |
PRK05718 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
11-217 |
1.22e-99 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 235577 Cd Length: 212 Bit Score: 287.91 E-value: 1.22e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 11 YHRERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQ 90
Cdd:PRK05718 3 NWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 91 VEAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTG 170
Cdd:PRK05718 83 AIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1862651764 171 GIRRNTAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:PRK05718 163 GISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVA 209
|
|
| eda |
TIGR01182 |
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ... |
16-217 |
6.33e-89 |
|
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: 260.32 E-value: 6.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 16 VRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAG 95
Cdd:TIGR01182 1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 96 AQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRN 175
Cdd:TIGR01182 81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1862651764 176 TAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALE 202
|
|
| Eda |
COG0800 |
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ... |
13-217 |
3.17e-83 |
|
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: 246.15 E-value: 3.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 13 RERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKA-IPDAWVGAGTVTSIAQYRQV 91
Cdd:COG0800 2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEvGPDALVGAGTVLTPEQARAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 92 EAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAgGIPALKAFSGPFPDVTFCPTGG 171
Cdd:COG0800 82 IAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTGG 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1862651764 172 IRRNTAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:COG0800 161 VSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
|
|
| Aldolase |
pfam01081 |
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ... |
16-211 |
3.55e-83 |
|
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: 245.46 E-value: 3.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 16 VRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAG 95
Cdd:pfam01081 1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 96 AQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRN 175
Cdd:pfam01081 81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1862651764 176 TAADYLALGNVQAVGGTWLTPADVVAAKDWSQITEI 211
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
|
|
| KDPG_aldolase |
cd00452 |
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ... |
20-211 |
1.50e-70 |
|
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: 213.15 E-value: 1.50e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 20 LQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAGAQFV 99
Cdd:cd00452 1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 100 ITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAgGIPALKAFSGPFPDVTFCPTGGIRRNTAAD 179
Cdd:cd00452 81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159
|
170 180 190
....*....|....*....|....*....|..
gi 1862651764 180 YLALGnVQAVGGTWLTPADVVAAKDWSQITEI 211
Cdd:cd00452 160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
|
|
| PRK06015 |
PRK06015 |
2-dehydro-3-deoxy-phosphogluconate aldolase; |
20-217 |
6.77e-67 |
|
2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 168348 Cd Length: 201 Bit Score: 204.66 E-value: 6.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 20 LQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAGAQFV 99
Cdd:PRK06015 1 LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 100 ITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFCPTGGIRRNTAAD 179
Cdd:PRK06015 81 VSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARD 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1862651764 180 YLALGNVQAVGGTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:PRK06015 161 YLSLPNVVCVGGSWVAPKELVAAGDWAGITKLAAEAAA 198
|
|
| PRK06552 |
PRK06552 |
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional |
20-213 |
8.38e-25 |
|
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
Pssm-ID: 180618 Cd Length: 213 Bit Score: 96.99 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 20 LQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVR---KAIPDAWVGAGTVTSIAQYRQVEAAGA 96
Cdd:PRK06552 10 LKANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVelyKDDPEVLIGAGTVLDAVTARLAILAGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 97 QFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGgiPA-LKAFSGPFPDVTFCPTGGIRRN 175
Cdd:PRK06552 90 QFIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLG--PSfIKAIKGPLPQVNVMVTGGVNLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1862651764 176 TAADYLALGnVQAV--GGTWLTPAdvvAAKDWSQITEIAR 213
Cdd:PRK06552 168 NVKDWFAAG-ADAVgiGGELNKLA---SQGDFDLITEKAK 203
|
|
| PRK07455 |
PRK07455 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
8-190 |
1.70e-24 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 180985 Cd Length: 187 Bit Score: 95.49 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 8 LSDYHRERVRAVLQSSplvpviaiqDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPDAWVGAGTVTSIAQ 87
Cdd:PRK07455 6 LAQLQQHRAIAVIRAP---------DLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 88 YRQVEAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVAGGIPALKAFSGPFPDVTFC 167
Cdd:PRK07455 77 LEEAIAAGAQFCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLI 156
|
170 180
....*....|....*....|...
gi 1862651764 168 PTGGIRRNTAADYLALGNVqAVG 190
Cdd:PRK07455 157 PTGGVTLENAQAFIQAGAI-AVG 178
|
|
| PRK09140 |
PRK09140 |
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed |
27-184 |
7.02e-23 |
|
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
Pssm-ID: 181670 Cd Length: 206 Bit Score: 91.43 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 27 PVIAIqdL-----DDAVPLCQALVDGGINVLEITLRTEHGLKAIEEVRKAIPD-AWVGAGTVTSIAQYRQVEAAGAQFVI 100
Cdd:PRK09140 11 PLIAI--LrgitpDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDrALIGAGTVLSPEQVDRLADAGGRLIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 101 TPGVTEAIL----EFGLTSeaplLPGIATISEMMVGYNLGYREFKFFPAEVAG--GIPALKAFSgPfPDVTFCPTGGIRR 174
Cdd:PRK09140 89 TPNTDPEVIrravALGMVV----MPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVL-P-PDVPVFAVGGVTP 162
|
170
....*....|
gi 1862651764 175 NTAADYLALG 184
Cdd:PRK09140 163 ENLAPYLAAG 172
|
|
| PRK07114 |
PRK07114 |
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase; |
11-217 |
2.25e-21 |
|
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
Pssm-ID: 235939 Cd Length: 222 Bit Score: 88.16 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 11 YHRERVRAVLQSSPLVPVIAIQDLDDAVPLCQALVDGGINVLEITLRTEHGLKAIEE----VRKAIPDAWVGAGTVTSIA 86
Cdd:PRK07114 3 FDRIAVLTAMKATGMVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVFAElvkyAAKELPGMILGVGSIVDAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 87 QYRQVEAAGAQFVITPGVTEAILEFGLTSEAPLLPGIATISEMMVGYNLGYREFKFFPAEVaGGIPALKAFSGPFPDVTF 166
Cdd:PRK07114 83 TAALYIQLGANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGSV-YGPGFVKAIKGPMPWTKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1862651764 167 CPTGGI---RRNTAADYLAlgNVQAVG-GTWLTPADVVAAKDWSQITEIARGSLA 217
Cdd:PRK07114 162 MPTGGVeptEENLKKWFGA--GVTCVGmGSKLIPKEALAAKDYAGIEQKVREALA 214
|
|
| IMPDH |
cd00381 |
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ... |
25-103 |
5.07e-04 |
|
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: 40.19 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1862651764 25 LVPVIAIQDLDDAVPLCQALVDGGINVleITLRTEHG-----LKAIEEVRKAIPDAWVGAGTVTSIAQYRQVEAAGAQFV 99
Cdd:cd00381 83 LLVGAAVGTREDDKERAEALVEAGVDV--IVIDSAHGhsvyvIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGV 160
|
....*..
gi 1862651764 100 ---ITPG 103
Cdd:cd00381 161 kvgIGPG 167
|
|
| |
