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Conserved domains on  [gi|505178899|ref|WP_015366001|]
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MULTISPECIES: bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase [Klebsiella]

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

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
1-213 1.67e-124

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


:

Pssm-ID: 235577  Cd Length: 212  Bit Score: 350.31  E-value: 1.67e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   1 MKNWKTTAEAILTNGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  81 KAVTEAGAQFAISPGLTESLLKAATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFC 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQ-EGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFC 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505178899 161 PTGGISPANYRDYLALNSVLCIGGSWLVPADALENGDYDRITKLAREAVEGAK 213
Cdd:PRK05718 160 PTGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
1-213 1.67e-124

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 350.31  E-value: 1.67e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   1 MKNWKTTAEAILTNGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  81 KAVTEAGAQFAISPGLTESLLKAATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFC 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQ-EGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFC 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505178899 161 PTGGISPANYRDYLALNSVLCIGGSWLVPADALENGDYDRITKLAREAVEGAK 213
Cdd:PRK05718 160 PTGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
26-212 1.21e-95

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: 277.27  E-value: 1.21e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   26 LEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:TIGR01182  19 VDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAGAQFIVSPGLTPELAKHAQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  106 gEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNSVLCIGGS 185
Cdd:TIGR01182  99 -DHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLANARDYLALPNVACGGGS 177
                         170       180
                  ....*....|....*....|....*..
gi 505178899  186 WLVPADALENGDYDRITKLAREAVEGA 212
Cdd:TIGR01182 178 WLVPKDLIAAGDWDEITRLAREALEII 204
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
9-204 1.90e-94

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: 273.97  E-value: 1.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899    9 EAILTNGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGA 88
Cdd:pfam01081   2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   89 QFAISPGLTESLLKAATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPA 168
Cdd:pfam01081  82 QFVVSPGLTADLLKHAV-DVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 505178899  169 NYRDYLALNSVLCIGGSWLVPADALENGDYDRITKL 204
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
27-213 2.96e-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: 248.46  E-value: 2.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEV-PEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:COG0800   24 EDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAAIAAGARFIVSPGLDPEVIKAAN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 106 GEGtIPLIPGISTVSELMLGMQYGLKEFKFFPAEAnGGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNSVLCIGGS 185
Cdd:COG0800  104 RAG-LPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTGGVSPDNAADYLAAGAVAVGGGS 181
                        170       180
                 ....*....|....*....|....*...
gi 505178899 186 WLVPADALENGDYDRITKLAREAVEGAK 213
Cdd:COG0800  182 WLVPKGAIAAGDWAAITERAREAVAAVR 209
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
27-204 2.99e-74

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: 222.39  E-value: 2.99e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAATG 106
Cdd:cd00452   16 EDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIVSPGLDPEVVKAANR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 107 EGtIPLIPGISTVSELMLGMQYGLKEFKFFPAEANgGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNsVLCIGGSW 186
Cdd:cd00452   96 AG-IPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEWLAAG-VVAVGGGS 172
                        170
                 ....*....|....*...
gi 505178899 187 LVPADALENGDYDRITKL 204
Cdd:cd00452  173 LLPKDAVAAGDWAAITAL 190
 
Name Accession Description Interval E-value
PRK05718 PRK05718
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
1-213 1.67e-124

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


Pssm-ID: 235577  Cd Length: 212  Bit Score: 350.31  E-value: 1.67e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   1 MKNWKTTAEAILTNGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQL 80
Cdd:PRK05718   1 MKNWKTSIEEILRAGPVVPVIVINKLEDAVPLAKALVAGGLPVLEVTLRTPAALEAIRLIAKEVPEALIGAGTVLNPEQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  81 KAVTEAGAQFAISPGLTESLLKAATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFC 160
Cdd:PRK05718  81 AQAIEAGAQFIVSPGLTPPLLKAAQ-EGPIPLIPGVSTPSELMLGMELGLRTFKFFPAEASGGVKMLKALAGPFPDVRFC 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505178899 161 PTGGISPANYRDYLALNSVLCIGGSWLVPADALENGDYDRITKLAREAVEGAK 213
Cdd:PRK05718 160 PTGGISPANYRDYLALPNVLCIGGSWMVPKDAIENGDWDRITRLAREAVALAK 212
eda TIGR01182
Entner-Doudoroff aldolase; 2-deydro-3-deoxyphosphogluconate aldolase (EC 4.1.2.14) is an ...
26-212 1.21e-95

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: 277.27  E-value: 1.21e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   26 LEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:TIGR01182  19 VDDALPLAKALIEGGLRVLEVTLRTPVALDAIRLLRKEVPDALIGAGTVLNPEQLRQAVAAGAQFIVSPGLTPELAKHAQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  106 gEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNSVLCIGGS 185
Cdd:TIGR01182  99 -DHGIPIIPGVATPSEIMLALELGITALKLFPAEVSGGVKMLKALAGPFPQVRFCPTGGINLANARDYLALPNVACGGGS 177
                         170       180
                  ....*....|....*....|....*..
gi 505178899  186 WLVPADALENGDYDRITKLAREAVEGA 212
Cdd:TIGR01182 178 WLVPKDLIAAGDWDEITRLAREALEII 204
Aldolase pfam01081
KDPG and KHG aldolase; This family includes the following members: 4-hydroxy-2-oxoglutarate ...
9-204 1.90e-94

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: 273.97  E-value: 1.90e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899    9 EAILTNGPVVPVIVVKKLEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGA 88
Cdd:pfam01081   2 ESILKEAKIVPVIVIKDKEDALPLAEALAAGGIRVLEVTLRTPCALDAIRLLRKNRPDALVGAGTVLNAQQLAEAAEAGA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899   89 QFAISPGLTESLLKAATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPA 168
Cdd:pfam01081  82 QFVVSPGLTADLLKHAV-DVKIPLIPGVSTPSEIMLGLDLGLTRFKFFPAEASGGVPAIKALAGPFPQVRFCPTGGIHPA 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 505178899  169 NYRDYLALNSVLCIGGSWLVPADALENGDYDRITKL 204
Cdd:pfam01081 161 NVRDYLALPNILCVGGSWLVPASLIQKGDWDRITAL 196
Eda COG0800
2-keto-3-deoxy-6-phosphogluconate aldolase [Carbohydrate transport and metabolism]; ...
27-213 2.96e-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: 248.46  E-value: 2.96e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEV-PEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:COG0800   24 EDAVPLAEALVAGGIRAIEVTLRTPAALEAIRALAKEVgPDALVGAGTVLTPEQARAAIAAGARFIVSPGLDPEVIKAAN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 106 GEGtIPLIPGISTVSELMLGMQYGLKEFKFFPAEAnGGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNSVLCIGGS 185
Cdd:COG0800  104 RAG-LPVLPGVATPTEIMAALEAGADAVKLFPAEA-LGPAYLKALKGPLPDVPFMPTGGVSPDNAADYLAAGAVAVGGGS 181
                        170       180
                 ....*....|....*....|....*...
gi 505178899 186 WLVPADALENGDYDRITKLAREAVEGAK 213
Cdd:COG0800  182 WLVPKGAIAAGDWAAITERAREAVAAVR 209
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
27-204 2.99e-74

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: 222.39  E-value: 2.99e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAATG 106
Cdd:cd00452   16 EDALALAEALIEGGIRAIEITLRTPGALEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFIVSPGLDPEVVKAANR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 107 EGtIPLIPGISTVSELMLGMQYGLKEFKFFPAEANgGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNsVLCIGGSW 186
Cdd:cd00452   96 AG-IPLLPGVATPTEIMQALELGADIVKLFPAEAV-GPAYIKALKGPFPQVRFMPTGGVSLDNAAEWLAAG-VVAVGGGS 172
                        170
                 ....*....|....*...
gi 505178899 187 LVPADALENGDYDRITKL 204
Cdd:cd00452  173 LLPKDAVAAGDWAAITAL 190
PRK06015 PRK06015
2-dehydro-3-deoxy-phosphogluconate aldolase;
26-208 1.23e-67

2-dehydro-3-deoxy-phosphogluconate aldolase;


Pssm-ID: 168348  Cd Length: 201  Bit Score: 206.20  E-value: 1.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  26 LEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:PRK06015  15 VEHAVPLARALAAGGLPAIEITLRTPAALDAIRAVAAEVEEAIVGAGTILNAKQFEDAAKAGSRFIVSPGTTQELLAAAN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 106 GEgTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNSVLCIGGS 185
Cdd:PRK06015  95 DS-DVPLLPGAATPSEVMALREEGYTVLKFFPAEQAGGAAFLKALSSPLAGTFFCPTGGISLKNARDYLSLPNVVCVGGS 173
                        170       180
                 ....*....|....*....|...
gi 505178899 186 WLVPADALENGDYDRITKLAREA 208
Cdd:PRK06015 174 WVAPKELVAAGDWAGITKLAAEA 196
PRK07455 PRK07455
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
26-174 9.35e-34

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


Pssm-ID: 180985  Cd Length: 187  Bit Score: 118.99  E-value: 9.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  26 LEHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:PRK07455  23 LELGLQMAEAVAAGGMRLIEITWNSDQPAELISQLREKLPECIIGTGTILTLEDLEEAIAAGAQFCFTPHVDPELIEAAV 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505178899 106 GEGtIPLIPGISTVSELMLGMQYGLKEFKFFPAEANGGVKALQAIAGPFGHIRFCPTGGISPANYRDYL 174
Cdd:PRK07455 103 AQD-IPIIPGALTPTEIVTAWQAGASCVKVFPVQAVGGADYIKSLQGPLGHIPLIPTGGVTLENAQAFI 170
PRK06552 PRK06552
keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional
27-210 2.52e-28

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


Pssm-ID: 180618  Cd Length: 213  Bit Score: 105.85  E-value: 2.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIA---KEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKA 103
Cdd:PRK06552  25 EEALKISLAVIKGGIKAIEVTYTNPFASEVIKELVelyKDDPEVLIGAGTVLDAVTARLAILAGAQFIVSPSFNRETAKI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 104 ATgEGTIPLIPGISTVSELMLGMQYGLKEFKFFPAEANgGVKALQAIAGPFGHIRFCPTGGISPANYRDYLALNS-VLCI 182
Cdd:PRK06552 105 CN-LYQIPYLPGCMTVTEIVTALEAGSEIVKLFPGSTL-GPSFIKAIKGPLPQVNVMVTGGVNLDNVKDWFAAGAdAVGI 182
                        170       180
                 ....*....|....*....|....*...
gi 505178899 183 GGSWLVPAdalENGDYDRITKLAREAVE 210
Cdd:PRK06552 183 GGELNKLA---SQGDFDLITEKAKKYMS 207
PRK09140 PRK09140
2-dehydro-3-deoxy-6-phosphogalactonate aldolase; Reviewed
27-175 1.76e-23

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


Pssm-ID: 181670  Cd Length: 206  Bit Score: 92.97  E-value: 1.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  27 EHAVPMAKALVAGGVRVLEVTLRTECALEAIRAIAKEVP-EAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAAT 105
Cdd:PRK09140  22 DEALAHVGALIEAGFRAIEIPLNSPDPFDSIAALVKALGdRALIGAGTVLSPEQVDRLADAGGRLIVTPNTDPEVIRRAV 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178899 106 GEGTIpLIPGISTVSELMLGMQYGLKEFKFFPAEANG--GVKALQAIAGPfgHIRFCPTGGISPANYRDYLA 175
Cdd:PRK09140 102 ALGMV-VMPGVATPTEAFAALRAGAQALKLFPASQLGpaGIKALRAVLPP--DVPVFAVGGVTPENLAPYLA 170
PRK07114 PRK07114
bifunctional 4-hydroxy-2-oxoglutarate aldolase/2-dehydro-3-deoxy-phosphogluconate aldolase;
34-210 1.59e-22

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


Pssm-ID: 235939  Cd Length: 222  Bit Score: 90.85  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899  34 KALVAGGVRVLEVTLRTECALEA----IRAIAKEVPEAIVGAGTVTNVEQLKAVTEAGAQFAISPGLTESLLKAATGEGt 109
Cdd:PRK07114  34 KACYDGGARVFEFTNRGDFAHEVfaelVKYAAKELPGMILGVGSIVDAATAALYIQLGANFIVTPLFNPDIAKVCNRRK- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178899 110 IPLIPGISTVSELMLGMQYGLKEFKFFPAEAnGGVKALQAIAGPFGHIRFCPTGGISP--ANYRDYLALnSVLCIG-GSW 186
Cdd:PRK07114 113 VPYSPGCGSLSEIGYAEELGCEIVKLFPGSV-YGPGFVKAIKGPMPWTKIMPTGGVEPteENLKKWFGA-GVTCVGmGSK 190
                        170       180
                 ....*....|....*....|....
gi 505178899 187 LVPADALENGDYDRITKLAREAVE 210
Cdd:PRK07114 191 LIPKEALAAKDYAGIEQKVREALA 214
 
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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