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Conserved domains on  [gi|1148626609|ref|WP_077371743|]
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MULTISPECIES: bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Cobetia]

Protein Classification

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase( domain architecture ID 10792645)

bifunctional 4-hydroxy-2-oxoglutarate (KHG) aldolase/2-dehydro-3-deoxy-phosphogluconate (KDPG) aldolase is involved in the degradation of glucose via the Entner-Doudoroff pathway; catalyzes the reversible, stereospecific retro-aldol cleavage of KDPG to pyruvate and D-glyceraldehyde-3-phosphate

EC:  4.1.3.16|4.1.2.14
Gene Ontology:  GO:0016832|GO:0016833|GO:0016830

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 12-214 7.01e-119

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


:

Pssm-ID: 235577  Cd Length: 212  Bit Score: 336.44  E-value: 7.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  12 TTEIDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVE 91
Cdd:PRK05718    5 KTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  92 ELGVDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGI 171
Cdd:PRK05718   85 EAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTGGI 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1148626609 172 TLNNAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREA 214
Cdd:PRK05718  165 SPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREA 207
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 12-214 7.01e-119

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 235577  Cd Length: 212  Bit Score: 336.44  E-value: 7.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  12 TTEIDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVE 91
Cdd:PRK05718    5 KTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  92 ELGVDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGI 171
Cdd:PRK05718   85 EAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTGGI 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1148626609 172 TLNNAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREA 214
Cdd:PRK05718  165 SPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREA 207
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 15-218 1.02e-97

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: 282.66  E-value: 1.02e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  15 IDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELG 94
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  95 VDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLN 174
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1148626609 175 NAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREASERF 218
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 12-216 4.05e-94

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: 273.88  E-value: 4.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  12 TTEIDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREAL-PNASIGAGTVLTPEQYRKV 90
Cdd:COG0800     2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  91 EELGVDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAgGVNAIKSFGGPISEARFCPTGG 170
Cdd:COG0800    82 IAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1148626609 171 ITLNNAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREASE 216
Cdd:COG0800   161 VSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 15-210 3.10e-87

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: 255.86  E-value: 3.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  15 IDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELG 94
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  95 VDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLN 174
Cdd:pfam01081  81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1148626609 175 NAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIREL 210
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 20-210 3.40e-80

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: 237.80  E-value: 3.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  20 QKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELGVDFVV 99
Cdd:cd00452     2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609 100 TPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAgGVNAIKSFGGPISEARFCPTGGITLNNAGDY 179
Cdd:cd00452    82 SPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEW 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1148626609 180 LALkNVMCVGGSWVAPQKLIDAGDWDGIREL 210
Cdd:cd00452   161 LAA-GVVAVGGGSLLPKDAVAAGDWAAITAL 190
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 12-214 7.01e-119

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 235577  Cd Length: 212  Bit Score: 336.44  E-value: 7.01e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  12 TTEIDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVE 91
Cdd:PRK05718    5 KTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  92 ELGVDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGI 171
Cdd:PRK05718   85 EAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTGGI 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1148626609 172 TLNNAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREA 214
Cdd:PRK05718  165 SPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREA 207
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 15-218 1.02e-97

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: 282.66  E-value: 1.02e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  15 IDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELG 94
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  95 VDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLN 174
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1148626609 175 NAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREASERF 218
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 12-216 4.05e-94

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: 273.88  E-value: 4.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  12 TTEIDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREAL-PNASIGAGTVLTPEQYRKV 90
Cdd:COG0800     2 KMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  91 EELGVDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAgGVNAIKSFGGPISEARFCPTGG 170
Cdd:COG0800    82 IAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTGG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1148626609 171 ITLNNAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIRELAREASE 216
Cdd:COG0800   161 VSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVA 206
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 15-210 3.10e-87

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: 255.86  E-value: 3.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  15 IDSICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELG 94
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  95 VDFVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLN 174
Cdd:pfam01081  81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1148626609 175 NAGDYLALKNVMCVGGSWVAPQKLIDAGDWDGIREL 210
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 20-210 3.40e-80

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: 237.80  E-value: 3.40e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  20 QKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELGVDFVV 99
Cdd:cd00452     2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609 100 TPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAgGVNAIKSFGGPISEARFCPTGGITLNNAGDY 179
Cdd:cd00452    82 SPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEW 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1148626609 180 LALkNVMCVGGSWVAPQKLIDAGDWDGIREL 210
Cdd:cd00452   161 LAA-GVVAVGGGSLLPKDAVAAGDWAAITAL 190
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
24-215 1.62e-78

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 233.94  E-value: 1.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  24 VLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELGVDFVVTPGT 103
Cdd:PRK06015    6 VIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFIVSPGT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609 104 TEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLNNAGDYLALK 183
Cdd:PRK06015   86 TQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARDYLSLP 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1148626609 184 NVMCVGGSWVAPQKLIDAGDWDGIRELAREAS 215
Cdd:PRK06015  166 NVVCVGGSWVAPKELVAAGDWAGITKLAAEAA 197
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
17-180 2.10e-38

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 180985  Cd Length: 187  Bit Score: 131.32  E-value: 2.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  17 SICQKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALPNASIGAGTVLTPEQYRKVEELGVD 96
Cdd:PRK07455    7 AQLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  97 FVVTPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAGGVNAIKSFGGPISEARFCPTGGITLNNA 176
Cdd:PRK07455   87 FCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENA 166


                  ....
gi 1148626609 177 GDYL 180
Cdd:PRK07455  167 QAFI 170
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 20-219 1.86e-27

keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional


Pssm-ID: 180618  Cd Length: 213  Bit Score: 103.92  E-value: 1.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  20 QKASVLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREAL---PNASIGAGTVLTPEQYRKVEELGVD 96
Cdd:PRK06552   11 KANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELYkddPEVLIGAGTVLDAVTARLAILAGAQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  97 FVVTPGTTEA------LYQygvtssVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAgGVNAIKSFGGPISEARFCPTGG 170
Cdd:PRK06552   91 FIVSPSFNREtakicnLYQ------IPYLPGCMTVTEIVTALEAGSEIVKLFPGSTL-GPSFIKAIKGPLPQVNVMVTGG 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1148626609 171 ITLNNAGDYLALKNVMC-VGGSWVAPQKLidaGDWDGIRELAREASERFH 219
Cdd:PRK06552  164 VNLDNVKDWFAAGADAVgIGGELNKLASQ---GDFDLITEKAKKYMSSLR 210
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 25-181 1.53e-25

2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed


Pssm-ID: 181670  Cd Length: 206  Bit Score: 98.75  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  25 LPVIAVER---IEDAVPLGKALYEGGLTVLEVTLRTDCALEAIRRMREALP-NASIGAGTVLTPEQYRKVEELGVDFVVT 100
Cdd:PRK09140   10 LPLIAILRgitPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGdRALIGAGTVLSPEQVDRLADAGGRLIVT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609 101 PGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEAAG--GVNAIKSFGGPisEARFCPTGGITLNNAGD 178
Cdd:PRK09140   90 PNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVLPP--DVPVFAVGGVTPENLAP 167


                  ...
gi 1148626609 179 YLA 181
Cdd:PRK09140  168 YLA 170
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
24-214 2.36e-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: 2.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  24 VLPVIAVERIEDAVPLGKALYEGGLTVLEVTLRTDCALEA----IRRMREALPNASIGAGTVLTPEQYRKVEELGVDFVV 99
Cdd:PRK07114   17 MVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVfaelVKYAAKELPGMILGVGSIVDAATAALYIQLGANFIV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609 100 TPGTTEALYQYGVTSSVPMLPGVATVSELMTGWQYGYRRFKFFPAEaAGGVNAIKSFGGPISEARFCPTGGITLN----- 174
Cdd:PRK07114   97 TPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGS-VYGPGFVKAIKGPMPWTKIMPTGGVEPTeenlk 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1148626609 175 ---NAGdylalknVMCVG-GSWVAPQKLIDAGDWDGIRELAREA 214
Cdd:PRK07114  176 kwfGAG-------VTCVGmGSKLIPKEALAAKDYAGIEQKVREA 212
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 34-127 3.51e-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: 40.58  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148626609  34 EDAVPLGKALYEGGLTVLEVtlrtDCA-------LEAIRRMREALPNASIGAGTVLTPEQYRKVEELGVDFV---VTPG- 102
Cdd:cd00381    93 EDDKERAEALVEAGVDVIVI----DSAhghsvyvIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVkvgIGPGs 168

                          90       100
                  ....*....|....*....|....*..
gi 1148626609 103 --TTEAlyQYGVtsSVPMLPGVATVSE 127
Cdd:cd00381   169 icTTRI--VTGV--GVPQATAVADVAA 191
PLN02875 PLN02875
4-hydroxyphenylpyruvate dioxygenase
 55-95 7.50e-03

4-hydroxyphenylpyruvate dioxygenase


Pssm-ID: 215472 [Multi-domain]  Cd Length: 398  Bit Score: 36.96  E-value: 7.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1148626609  55 LRTDCALEAIRRMR--------EALPNASIG--------AGTVLTPEQYRKVEELGV 95
Cdd:PLN02875  268 LKSDDIFGTLREMRarshiggfEFMPPPPPTyyknlkkrVGDVLTEEQIKECEELGI 324
 
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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