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Conserved domains on  [gi|504402767|ref|WP_014589869|]
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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 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
 13-224 8.01e-125

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


:

Pssm-ID: 235577  Cd Length: 212  Bit Score: 351.85  E-value: 8.01e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  13 MADKAARIDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMF 92
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  93 AAVEAAGAQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCP 172
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504402767 173 TGGVNPANVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMALLD 224
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 13-224 8.01e-125

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 351.85  E-value: 8.01e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  13 MADKAARIDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMF 92
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  93 AAVEAAGAQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCP 172
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504402767 173 TGGVNPANVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMALLD 224
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 20-215 1.71e-114

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: 325.20  E-value: 1.71e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767   20 IDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAG 99
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  100 AQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPA 179
Cdd:pfam01081  81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 504402767  180 NVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEAC 215
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 20-222 7.69e-92

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: 268.03  E-value: 7.69e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767   20 IDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAG 99
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  100 AQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPA 179
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 504402767  180 NVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMAL 222
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEI 203
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 16-226 2.18e-84

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: 249.61  E-value: 2.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  16 KAARIDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQR-PELCVGAGTVLDRSMFAA 94
Cdd:COG0800    1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  95 VEAAGAQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISgGVAAIKAFGGPFGDIRFCPTG 174
Cdd:COG0800   81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504402767 175 GVNPANVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMALLDAI 226
Cdd:COG0800  160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRAA 211
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 25-214 1.63e-75

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: 226.25  E-value: 1.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  25 KKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAGAQFVV 104
Cdd:cd00452    2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 105 TPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISgGVAAIKAFGGPFGDIRFCPTGGVNPANVRNY 184
Cdd:cd00452   82 SPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEW 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 504402767 185 MALPnVMCVGGTWMLDSSWIKNGDWARIEA 214
Cdd:cd00452  161 LAAG-VVAVGGGSLLPKDAVAAGDWAAITA 189
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 13-224 8.01e-125

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 351.85  E-value: 8.01e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  13 MADKAARIDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMF 92
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  93 AAVEAAGAQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCP 172
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQEGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFCP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504402767 173 TGGVNPANVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMALLD 224
Cdd:PRK05718 161 TGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
 20-215 1.71e-114

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: 325.20  E-value: 1.71e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767   20 IDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAG 99
Cdd:pfam01081   1 IESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  100 AQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPA 179
Cdd:pfam01081  81 AQFVVSPGLTADLLKHAVDVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 504402767  180 NVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEAC 215
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
 20-222 7.69e-92

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: 268.03  E-value: 7.69e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767   20 IDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAG 99
Cdd:TIGR01182   1 IEELLREAKIVPVIRIDDVDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  100 AQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPA 179
Cdd:TIGR01182  81 AQFIVSPGLTPELAKHAQDHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 504402767  180 NVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMAL 222
Cdd:TIGR01182 161 NARDYLALPNVACGGGSWLVPKDLIAAGDWDEITRLAREALEI 203
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
 16-226 2.18e-84

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: 249.61  E-value: 2.18e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  16 KAARIDAICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQR-PELCVGAGTVLDRSMFAA 94
Cdd:COG0800    1 SKMELLELLAAAPVVPVLRGDDPEDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  95 VEAAGAQFVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISgGVAAIKAFGGPFGDIRFCPTG 174
Cdd:COG0800   81 AIAAGARFIVSPGLDPEVIKAANRAGLPVLPGVATPTEIMAALEAGADAVKLFPAEAL-GPAYLKALKGPLPDVPFMPTG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504402767 175 GVNPANVRNYMALPNVMCVGGTWMLDSSWIKNGDWARIEACSAEAMALLDAI 226
Cdd:COG0800  160 GVSPDNAADYLAAGAVAVGGGSWLVPKGAIAAGDWAAITERAREAVAAVRAA 211
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
 25-214 1.63e-75

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: 226.25  E-value: 1.63e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  25 KKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAGAQFVV 104
Cdd:cd00452    2 KAQPLVAVLRGDDAEDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 105 TPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISgGVAAIKAFGGPFGDIRFCPTGGVNPANVRNY 184
Cdd:cd00452   82 SPGLDPEVVKAANRAGIPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEW 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 504402767 185 MALPnVMCVGGTWMLDSSWIKNGDWARIEA 214
Cdd:cd00452  161 LAAG-VVAVGGGSLLPKDAVAAGDWAAITA 189
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
29-222 3.97e-67

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 205.43  E-value: 3.97e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  29 ILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAGAQFVVTPGI 108
Cdd:PRK06015   6 VIPVLLIDDVEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFIVSPGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 109 TQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPANVRNYMALP 188
Cdd:PRK06015  86 TQELLAAANDSDVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARDYLSLP 165

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504402767 189 NVMCVGGTWMLDSSWIKNGDWARIEACSAEAMAL 222
Cdd:PRK06015 166 NVVCVGGSWVAPKELVAAGDWAGITKLAAEAAAL 199
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
22-185 1.56e-36

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


Pssm-ID: 180985  Cd Length: 187  Bit Score: 126.69  E-value: 1.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  22 AICKKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELCVGAGTVLDRSMFAAVEAAGAQ 101
Cdd:PRK07455   7 AQLQQHRAIAVIRAPDLELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 102 FVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGGVAAIKAFGGPFGDIRFCPTGGVNPANV 181
Cdd:PRK07455  87 FCFTPHVDPELIEAAVAQDIPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENA 166


                 ....
gi 504402767 182 RNYM 185
Cdd:PRK07455 167 QAFI 170
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
 25-226 2.82e-28

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 106.23  E-value: 2.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  25 KKARILPVITIAREEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQ---RPELCVGAGTVLDRSMFAAVEAAGAQ 101
Cdd:PRK06552  11 KANGVVAVVRGESKEEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVELykdDPEVLIGAGTVLDAVTARLAILAGAQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 102 FVVTPGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISGgVAAIKAFGGPFGDIRFCPTGGVNPANV 181
Cdd:PRK06552  91 FIVSPSFNRETAKICNLYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTLG-PSFIKAIKGPLPQVNVMVTGGVNLDNV 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504402767 182 RNYMALPNVMC-VGGTWMLDSswiKNGDWARIEACSAEAMALLDAI 226
Cdd:PRK06552 170 KDWFAAGADAVgIGGELNKLA---SQGDFDLITEKAKKYMSSLRKA 212
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
 30-186 2.42e-21

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 87.57  E-value: 2.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  30 LPVITIAR---EEDILPLADALAAGGIRTLEVTLRSQHGLKAIQVLREQRPELC-VGAGTVLDRSMFAAVEAAGAQFVVT 105
Cdd:PRK09140  10 LPLIAILRgitPDEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGDRAlIGAGTVLSPEQVDRLADAGGRLIVT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 106 PGITQDILEAGVDSEIPLLPGISTPSEIMMGYALGYRRFKLFPAEISG--GVAAIKAFGGPfgDIRFCPTGGVNPANVRN 183
Cdd:PRK09140  90 PNTDPEVIRRAVALGMVVMPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVLPP--DVPVFAVGGVTPENLAP 167


                 ...
gi 504402767 184 YMA 186
Cdd:PRK09140 168 YLA 170
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
46-226 1.07e-19

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


Pssm-ID: 235939  Cd Length: 222  Bit Score: 83.92  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  46 DALAAGGIRTLEVTLRsqhGLKAIQVLRE-------QRPELCVGAGTVLDRSMFAAVEAAGAQFVVTPGITQDILEAGVD 118
Cdd:PRK07114  34 KACYDGGARVFEFTNR---GDFAHEVFAElvkyaakELPGMILGVGSIVDAATAALYIQLGANFIVTPLFNPDIAKVCNR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767 119 SEIPLLPGISTPSEIMMGYALGYRRFKLFPAEIsGGVAAIKAFGGPFGDIRFCPTGGVNP--ANVRNYMAlPNVMCVG-G 195
Cdd:PRK07114 111 RKVPYSPGCGSLSEIGYAEELGCEIVKLFPGSV-YGPGFVKAIKGPMPWTKIMPTGGVEPteENLKKWFG-AGVTCVGmG 188

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504402767 196 TWMLDSSWIKNGDWARIEACSAEAMALLDAI 226
Cdd:PRK07114 189 SKLIPKEALAAKDYAGIEQKVREALAIIKEV 219
RESC5 cd23678
RNA-editing substrate-binding complex subunit 5 (RESC5); RESC5 (GRBC5, MRB11870) is a ...
 25-79 8.09e-05

RNA-editing substrate-binding complex subunit 5 (RESC5); RESC5 (GRBC5, MRB11870) is a component of the RNA-editing substrate-binding complex (RESC) that is composed of about 20 components and is involved in kinetoplast RNA processing. The mitochondrial DNA of Trypanosomatids, known as the kinetoplast DNA (kDNA or mtDNA), consists of a network of dozens of maxicircles and thousands of minicircles concatenated together. Maxicircles are equivalent to other eukaryotic mitochondrial DNAs, while minicircles encode guide RNAs (gRNAs) involved in U-insertion/deletion editing processes exclusive of Trypanosomatids that produce the maturation of the maxicircle-encoded transcripts. Although most gRNAs are encoded by minicircles, varying numbers of maxicircle-encoded gRNAs have been identified in kinetoplastids species. Trypanosoma brucei maxicircles encode 9S and 12S rRNAs, two gRNAs, two ribosomal proteins and 16 subunits of respiratory complexes. 12 of the 18 maxicircle genes are present as cryptogenes whose transcripts require U-insertion/deletion editing, mediated by gRNAs, to restore a protein-coding capacity. RESC interacts with two other complexes, the RNA-editing helicase 2 complex (REH2C) and RNA-editing catalytic complex (RECC) to form an assembly (editosome/holoenzyme) that carries out U-insertion/deletion mRNA editing. RESC5 is predicted (AlphaFold) to adopt a beta/alpha-propeller structure characteristic of the pentein superfamily, a mechanistically diverse superfamily encompassing both non-catalytic proteins and enzymes that catalyze hydrolase, dihydrolase and amidinotransfer reactions on guanidine substrates.


Pssm-ID: 467894  Cd Length: 278  Bit Score: 42.68  E-value: 8.09e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504402767  25 KKARILPVITIAREEDILPLADALAAGGIRTLeVTLRSQHGLKAIQVLREQRPEL 79
Cdd:cd23678  156 DQQRAFDVVTIEQEGDAPPLGDYFGFAGQRTL-LAWKDEHGLLAVDQAQQRIPKV 209
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 11-117 7.25e-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: 39.81  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504402767  11 LSMADKAARIDAIckKARILPVITIAREEDILPLADALAAGGIRTLevTLRSQHG-----LKAIQVLREQRPELCVGAGT 85
Cdd:cd00381   67 MSIEEQAEEVRKV--KGRLLVGAAVGTREDDKERAEALVEAGVDVI--VIDSAHGhsvyvIEMIKFIKKKYPNVDVIAGN 142

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504402767  86 VLDRSMFAAVEAAGAQFV---VTPG---ITQDILEAGV 117
Cdd:cd00381  143 VVTAEAARDLIDAGADGVkvgIGPGsicTTRIVTGVGV 180
 
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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