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Conserved domains on  [gi|527036661|ref|WP_020883402|]
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MULTISPECIES: bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Enterobacter]

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
 1-212 1.64e-136

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


:

Pssm-ID: 235577  Cd Length: 212  Bit Score: 380.74  E-value: 1.64e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   1 MKNWKTSAEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  81 ADVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCP 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527036661 161 TGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGAK 212
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 1-212 1.64e-136

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 380.74  E-value: 1.64e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   1 MKNWKTSAEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  81 ADVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCP 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527036661 161 TGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGAK 212
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 9-203 1.84e-107

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: 306.71  E-value: 1.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661    9 EAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGA 88
Cdd:pfam01081   2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   89 QFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPAN 168
Cdd:pfam01081  82 QFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPAN 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 527036661  169 YRDYLALKSVLCIGGSWLVPADALEAGDWDRITKL 203
Cdd:pfam01081 162 VRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 8-211 7.74e-106

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: 303.08  E-value: 7.74e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661    8 AEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAG 87
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   88 AQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPA 167
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 527036661  168 NYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGA 211
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 4-213 1.97e-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: 266.95  E-value: 1.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   4 WKTSAEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEV-PDAIIGAGTVLNAQQLAD 82
Cdd:COG0800    1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  83 VTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEAnGGTKALQAIAGPFSQVRFCPTG 162
Cdd:COG0800   81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 527036661 163 GISPANYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGAKQ 213
Cdd:COG0800  160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRA 210
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 12-203 7.63e-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: 236.65  E-value: 7.63e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  12 LTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGAQFA 91
Cdd:cd00452    1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  92 ISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANgGTKALQAIAGPFSQVRFCPTGGISPANYRD 171
Cdd:cd00452   81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 527036661 172 YLALKsVLCIGGSWLVPADALEAGDWDRITKL 203
Cdd:cd00452  160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 1-212 1.64e-136

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 380.74  E-value: 1.64e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   1 MKNWKTSAEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  81 ADVTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCP 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 527036661 161 TGGISPANYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGAK 212
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 9-203 1.84e-107

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: 306.71  E-value: 1.84e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661    9 EAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGA 88
Cdd:pfam01081   2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   89 QFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPAN 168
Cdd:pfam01081  82 QFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPAN 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 527036661  169 YRDYLALKSVLCIGGSWLVPADALEAGDWDRITKL 203
Cdd:pfam01081 162 VRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 8-211 7.74e-106

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: 303.08  E-value: 7.74e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661    8 AEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAG 87
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   88 AQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPA 167
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 527036661  168 NYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGA 211
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEII 204
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 4-213 1.97e-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: 266.95  E-value: 1.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   4 WKTSAEAILTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEV-PDAIIGAGTVLNAQQLAD 82
Cdd:COG0800    1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  83 VTEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEAnGGTKALQAIAGPFSQVRFCPTG 162
Cdd:COG0800   81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 527036661 163 GISPANYRDYLALKSVLCIGGSWLVPADALEAGDWDRITKLAREAVEGAKQ 213
Cdd:COG0800  160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRA 210
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 12-203 7.63e-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: 236.65  E-value: 7.63e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  12 LTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGAQFA 91
Cdd:cd00452    1 LKAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  92 ISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANgGTKALQAIAGPFSQVRFCPTGGISPANYRD 171
Cdd:cd00452   81 VSPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAE 159

                        170       180       190
                 ....*....|....*....|....*....|..
gi 527036661 172 YLALKsVLCIGGSWLVPADALEAGDWDRITKL 203
Cdd:cd00452  160 WLAAG-VVAVGGGSLLPKDAVAAGDWAAITAL 190
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
12-207 3.24e-77

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 230.47  E-value: 3.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  12 LTTGPVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGAQFA 91
Cdd:PRK06015   1 LKLQPVIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  92 ISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPANYRD 171
Cdd:PRK06015  81 VSPGTTQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARD 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 527036661 172 YLALKSVLCIGGSWLVPADALEAGDWDRITKLAREA 207
Cdd:PRK06015 161 YLSLPNVVCVGGSWVAPKELVAAGDWAGITKLAAEA 196
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
18-173 1.10e-32

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


Pssm-ID: 180985  Cd Length: 187  Bit Score: 116.29  E-value: 1.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  18 VPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGAQFAISPGLT 97
Cdd:PRK07455  15 IAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQFCFTPHVD 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036661  98 EPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANGGTKALQAIAGPFSQVRFCPTGGISPANYRDYL 173
Cdd:PRK07455  95 PELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENAQAFI 170
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 17-209 3.19e-31

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 113.17  E-value: 3.19e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  17 VVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIA---KEVPDAIIGAGTVLNAQQLADVTEAGAQFAIS 93
Cdd:PRK06552  15 VVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVelyKDDPEVLIGAGTVLDAVTARLAILAGAQFIVS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  94 PGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANgGTKALQAIAGPFSQVRFCPTGGISPANYRDYL 173
Cdd:PRK06552  95 PSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTL-GPSFIKAIKGPLPQVNVMVTGGVNLDNVKDWF 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 527036661 174 ALKS-VLCIGGSWLVPAdalEAGDWDRITKLAREAVE 209
Cdd:PRK06552 174 AAGAdAVGIGGELNKLA---SQGDFDLITEKAKKYMS 207
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
8-209 2.34e-26

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


Pssm-ID: 235939  Cd Length: 222  Bit Score: 100.87  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661   8 AEAILTTGpVVPVIVVNKLEHAVPMAKALVAGGVRVLEVTLRTACAMDA----IRAIAKEVPDAIIGAGTVLNAQQLADV 83
Cdd:PRK07114   9 LTAMKATG-MVPVFYHADVEVAKKVIKACYDGGARVFEFTNRGDFAHEVfaelVKYAAKELPGMILGVGSIVDAATAALY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  84 TEAGAQFAISPGLTEPLLKAATEGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEAnGGTKALQAIAGPFSQVRFCPTGG 163
Cdd:PRK07114  88 IQLGANFIVTPLFNPDIAKVCNRRKVPYSPGCGSLSEIGYAEELGCEIVKLFPGSV-YGPGFVKAIKGPMPWTKIMPTGG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 527036661 164 ISP--ANYRDYLAlKSVLCIG-GSWLVPADALEAGDWDRITKLAREAVE 209
Cdd:PRK07114 167 VEPteENLKKWFG-AGVTCVGmGSKLIPKEALAAKDYAGIEQKVREALA 214
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 27-174 2.93e-23

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 92.20  E-value: 2.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036661  27 EHAVPMAKALVAGGVRVLEVTLRTACAMDAIRAIAKEVPD-AIIGAGTVLNAQQLADVTEAGAQFAISPGLTEPLLKAAT 105
Cdd:PRK09140  22 DEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDrALIGAGTVLSPEQVDRLADAGGRLIVTPNTDPEVIRRAV 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036661 106 EGTIPLIPGISTVSELMMGMDYGLKEFKFFPAEANG--GTKALQAIAGPfsQVRFCPTGGISPANYRDYLA 174
Cdd:PRK09140 102 ALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVLPP--DVPVFAVGGVTPENLAPYLA 170
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 33-88 8.29e-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: 36.34  E-value: 8.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036661  33 AKALVAGGVRVLevTLRTACA-----MDAIRAIAKEVPDAIIGAGTVLNAQQLADVTEAGA 88
Cdd:cd00381   99 AEALVEAGVDVI--VIDSAHGhsvyvIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGA 157
 
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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