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Conserved domains on  [gi|501022383|ref|WP_012075046|]
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MULTISPECIES: bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Pseudomonas]

Protein Classification

bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase( domain architecture ID 11492077)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 6-209 4.26e-108

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: 308.86  E-value: 4.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383    6 DRVLLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAG 85
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   86 AQFAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLD 165
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 501022383  166 NLLNFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLA 209
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
 
Name Accession Description Interval E-value
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 6-209 4.26e-108

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: 308.86  E-value: 4.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383    6 DRVLLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAG 85
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   86 AQFAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLD 165
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 501022383  166 NLLNFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLA 209
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 9-209 2.02e-95

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 277.12  E-value: 2.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQF 88
Cdd:PRK05718  11 ILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQAIEAGAQF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  89 AVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLL 168
Cdd:PRK05718  91 IVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTGGISPANYR 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 501022383 169 NFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLA 209
Cdd:PRK05718 171 DYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALA 211
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 9-212 2.63e-92

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: 269.26  E-value: 2.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREV-PEVLLGAGTLIHTEQFLEARDAGAQ 87
Cdd:COG0800    8 LLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAAIAAGAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  88 FAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGVNLDNL 167
Cdd:COG0800   88 FIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAE-ALGPAYLKALKGPLPDVPFMPTGGVSPDNA 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501022383 168 LNFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLAGSL 212
Cdd:COG0800  167 ADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRAA 211
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 10-201 3.40e-82

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: 242.81  E-value: 3.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  10 LQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFA 89
Cdd:cd00452    1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  90 VSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLN 169
Cdd:cd00452   81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAE-AVGPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 501022383 170 FLRLPnVACVGGTWLAPPSLIRARAWDQITQL 201
Cdd:cd00452  160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 10-201 4.89e-74

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: 222.35  E-value: 4.89e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   10 LQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFA 89
Cdd:pfam01081   5 LKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGAQFV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   90 VSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLN 169
Cdd:pfam01081  85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPANVRD 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 501022383  170 FLRLPNVACVGGTWLAPPSLIRARAWDQITQL 201
Cdd:pfam01081 165 YLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
 
Name Accession Description Interval E-value
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 6-209 4.26e-108

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: 308.86  E-value: 4.26e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383    6 DRVLLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAG 85
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   86 AQFAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLD 165
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 501022383  166 NLLNFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLA 209
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 9-209 2.02e-95

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 277.12  E-value: 2.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQF 88
Cdd:PRK05718  11 ILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQLAQAIEAGAQF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  89 AVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLL 168
Cdd:PRK05718  91 IVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCPTGGISPANYR 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 501022383 169 NFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLA 209
Cdd:PRK05718 171 DYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALA 211
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 9-212 2.63e-92

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: 269.26  E-value: 2.63e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREV-PEVLLGAGTLIHTEQFLEARDAGAQ 87
Cdd:COG0800    8 LLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAAIAAGAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  88 FAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGVNLDNL 167
Cdd:COG0800   88 FIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAE-ALGPAYLKALKGPLPDVPFMPTGGVSPDNA 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501022383 168 LNFLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLAGSL 212
Cdd:COG0800  167 ADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRAA 211
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 10-201 3.40e-82

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: 242.81  E-value: 3.40e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  10 LQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFA 89
Cdd:cd00452    1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  90 VSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLN 169
Cdd:cd00452   81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAE-AVGPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 501022383 170 FLRLPnVACVGGTWLAPPSLIRARAWDQITQL 201
Cdd:cd00452  160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 10-201 4.89e-74

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: 222.35  E-value: 4.89e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   10 LQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFA 89
Cdd:pfam01081   5 LKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGAQFV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   90 VSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLN 169
Cdd:pfam01081  85 VSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPANVRD 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 501022383  170 FLRLPNVACVGGTWLAPPSLIRARAWDQITQL 201
Cdd:pfam01081 165 YLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
10-210 2.14e-70

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 213.14  E-value: 2.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  10 LQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFA 89
Cdd:PRK06015   1 LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  90 VSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLN 169
Cdd:PRK06015  81 VSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 501022383 170 FLRLPNVACVGGTWLAPPSLIRARAWDQITQLAREARDLAG 210
Cdd:PRK06015 161 YLSLPNVVCVGGSWVAPKELVAAGDWAGITKLAAEAAALKA 201
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 18-204 9.74e-36

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 125.11  E-value: 9.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  18 VLVI----EDVALApdLARALYAGGVTVLEVTLRTPQALDAI---AAIHREVPEVLLGAGTLIHTEQFLEARDAGAQFAV 90
Cdd:PRK06552  16 VAVVrgesKEEALK--ISLAVIKGGIKAIEVTYTNPFASEVIkelVELYKDDPEVLIGAGTVLDAVTARLAILAGAQFIV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  91 SPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGVNLDNLLNF 170
Cdd:PRK06552  94 SPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGS-TLGPSFIKAIKGPLPQVNVMVTGGVNLDNVKDW 172

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 501022383 171 LRLPNVAC-VGGTWLAPPSLIRaraWDQITQLARE 204
Cdd:PRK06552 173 FAAGADAVgIGGELNKLASQGD---FDLITEKAKK 204
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
9-187 4.40e-31

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


Pssm-ID: 180985  Cd Length: 187  Bit Score: 112.44  E-value: 4.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVPEVLLGAGTLIHTEQFLEARDAGAQF 88
Cdd:PRK07455   8 QLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  89 AVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASVKMLKSLKGPFTGIRFCPTGGVNLDNLL 168
Cdd:PRK07455  88 CFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENAQ 167

                        170
                 ....*....|....*....
gi 501022383 169 NFLRLPNVACVGGTWLAPP 187
Cdd:PRK07455 168 AFIQAGAIAVGLSGQLFPK 186
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
9-208 3.74e-27

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


Pssm-ID: 235939  Cd Length: 222  Bit Score: 103.18  E-value: 3.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383   9 LLQASPVLPVLVIEDVALAPDLARALYAGGVTVLEVTLRTPQALDAIAAIHR----EVPEVLLGAGTLIHTEQFLEARDA 84
Cdd:PRK07114  11 AMKATGMVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVFAELVKyaakELPGMILGVGSIVDAATAALYIQL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  85 GAQFAVSPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADgTASVKMLKSLKGPFTGIRFCPTGGV-- 162
Cdd:PRK07114  91 GANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGS-VYGPGFVKAIKGPMPWTKIMPTGGVep 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 501022383 163 NLDNLLNFLRlPNVACVG-GTWLAPPSLIRARAWDQITQLAREARDL 208
Cdd:PRK07114 170 TEENLKKWFG-AGVTCVGmGSKLIPKEALAAKDYAGIEQKVREALAI 215
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 27-171 8.08e-27

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 101.83  E-value: 8.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  27 APDLARALYAGGVTVLEVTLRTPQALDAIAAIHREVP-EVLLGAGTLIHTEQFLEARDAGAQFAVSPGCTPRLAAAAEDA 105
Cdd:PRK09140  24 ALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGdRALIGAGTVLSPEQVDRLADAGGRLIVTPNTDPEVIRRAVAL 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501022383 106 GLPYLPGVMTPSEVLLALEYGYRSLKLFPAD--GTASVKMLKSLKGPftGIRFCPTGGVNLDNLLNFL 171
Cdd:PRK09140 104 GMVVMPGVATPTEAFAALRAGAQALKLFPASqlGPAGIKALRAVLPP--DVPVFAVGGVTPENLAPYL 169
ASKHA_NBD_HSP70_ScSsz1p-like cd10232
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ...
 76-141 8.09e-03

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.


Pssm-ID: 466830 [Multi-domain]  Cd Length: 349  Bit Score: 36.57  E-value: 8.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501022383  76 EQFLEARDAGAQFAV----SPGCTPRLAAAAEDAGLPYLPGVMTPSEVLLALEYGYRSLKLFPADGTASV 141
Cdd:cd10232   94 EDYLGKKVTGAVLSVptdfTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAETSGDTIKDKTVVV 163
 
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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