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Conserved domains on  [gi|38704050|ref|NP_310927|]
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fructose-bisphosphate aldolase class I [Escherichia coli O157:H7 str. Sakai]

Protein Classification

class I fructose-bisphosphate aldolase( domain architecture ID 10013155)

class I fructose-bisphosphate aldolase catalyzes the conversion of beta-D-fructose 1,6-bisphosphate to D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09250 PRK09250
class I fructose-bisphosphate aldolase;
1-350 0e+00

class I fructose-bisphosphate aldolase;


:

Pssm-ID: 236431  Cd Length: 348  Bit Score: 673.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050    1 MTDIAQLLGKDADNLLQHRCmTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHS 80
Cdd:PRK09250   1 MTDIAMLLGKDADSLLSHRC-KIPKDQLHLPGPDFVDRVMIYSDRNPGVLRNLQRLLNHGRLAGTGYLSILPVDQGFEHS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   81 AGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMG 160
Cdd:PRK09250  80 AGASFAPNPLYFDPENIVKLAIEAGCNAVASTLGVLEAVARKYAHKIPFILKLNHNELLSYPNTYDQALTASVEDALRLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  161 AVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGvDYHVSADLTGQANHLAATIGADIVKQKM 240
Cdd:PRK09250 160 AVAVGATIYFGSEESRRQIEEISEAFEEAHELGLATVLWSYLRNSAFKKDG-DYHTAADLTGQANHLAATIGADIIKQKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  241 AENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILG 320
Cdd:PRK09250 239 PTNNGGYKAINFGKTDDRVYSKLTSDHPIDLVRYQVANCYMGRRGLINSGGASKGEDDLLDAVRTAVINKRAGGMGLIIG 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 38704050  321 RKAFKKSMADGVKLINAVQDVYLDSKITIA 350
Cdd:PRK09250 319 RKAFQRPMAEGVKLLNAIQDVYLDKKITIA 348
 
Name Accession Description Interval E-value
PRK09250 PRK09250
class I fructose-bisphosphate aldolase;
1-350 0e+00

class I fructose-bisphosphate aldolase;


Pssm-ID: 236431  Cd Length: 348  Bit Score: 673.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050    1 MTDIAQLLGKDADNLLQHRCmTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHS 80
Cdd:PRK09250   1 MTDIAMLLGKDADSLLSHRC-KIPKDQLHLPGPDFVDRVMIYSDRNPGVLRNLQRLLNHGRLAGTGYLSILPVDQGFEHS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   81 AGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMG 160
Cdd:PRK09250  80 AGASFAPNPLYFDPENIVKLAIEAGCNAVASTLGVLEAVARKYAHKIPFILKLNHNELLSYPNTYDQALTASVEDALRLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  161 AVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGvDYHVSADLTGQANHLAATIGADIVKQKM 240
Cdd:PRK09250 160 AVAVGATIYFGSEESRRQIEEISEAFEEAHELGLATVLWSYLRNSAFKKDG-DYHTAADLTGQANHLAATIGADIIKQKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  241 AENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILG 320
Cdd:PRK09250 239 PTNNGGYKAINFGKTDDRVYSKLTSDHPIDLVRYQVANCYMGRRGLINSGGASKGEDDLLDAVRTAVINKRAGGMGLIIG 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 38704050  321 RKAFKKSMADGVKLINAVQDVYLDSKITIA 350
Cdd:PRK09250 319 RKAFQRPMAEGVKLLNAIQDVYLDKKITIA 348
FbaB COG1830
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
48-344 1.18e-94

Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441435 [Multi-domain]  Cd Length: 259  Bit Score: 282.01  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  48 AVLRNMQTLYNtgrlAGTGYLSILPVDQGVEHSAgasfaaNPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRI 127
Cdd:COG1830   3 GKKIRLSRIFN----AGTGRLVIVAVDHGVEHGP------NPGLEDPEEIVRLAAEGGADAVALTKGILERLARKYARDI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 128 PFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAF 207
Cdd:COG1830  73 PLILKLNGSTSLGYPDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPYPRGPAV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 208 KKDGvdyhvSADLTGQANHLAATIGADIVKQKmaennggykainygYTDDrvyskltsenpIDLVRYQLANCYMgraGLI 287
Cdd:COG1830 153 KDET-----DPDLVAHAARIAAELGADIVKTK--------------YPGD-----------PESFREVVAACPV---PVV 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38704050 288 NSGGA-AGGETDLSDAVRTAVinkRAGGMGLILGRKAFKKSMADGVklINAVQDVYLD 344
Cdd:COG1830 200 IAGGPkTPDDEDFLEMVRDAI---DAGAAGVAVGRNIFQRPNPEAM--LRAISAIVHE 252
DhnA cd00958
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
68-343 4.44e-92

Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.


Pssm-ID: 188645 [Multi-domain]  Cd Length: 235  Bit Score: 274.86  E-value: 4.44e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  68 LSILPVDQGVEHSagasFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQ 147
Cdd:cd00958   1 LVILAVDHGIEHG----FGPNPGLEDPEETVKLAAEGGADAVALTKGIARAYGREYAGDIPLIVKLNGSTSLSPKDDNDK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 148 TLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKdgvdyHVSADLTGQANHL 227
Cdd:cd00958  77 VLVASVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVKN-----EKDPDLIAYAARI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 228 AATIGADIVKQKMAENNGGYKAINYGYTddrvyskltsenpidlvryqlancymgrAGLINSGGAagGETDLSDAVRTAV 307
Cdd:cd00958 152 GAELGADIVKTKYTGDAESFKEVVEGCP----------------------------VPVVIAGGP--KKDSEEEFLKMVY 201
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38704050 308 INKRAGGMGLILGRKAFKKSmaDGVKLINAVQDVYL 343
Cdd:cd00958 202 DAMEAGAAGVAVGRNIFQRP--DPVAMLRAISAVVH 235
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
68-326 4.04e-78

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 239.21  E-value: 4.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050    68 LSILPVDQGVEHSAGASFAanplYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQ 147
Cdd:pfam01791   1 TSILAMDQGVANGPDFAFA----LEDPKVLVAEAATPGANAVLLDPGFIARAHRGYGKDIGLIVALNHGTDLIPINGRDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   148 TLYASVEQAFNMGAVAVGATIYF---GSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGvdyhvSADLTGQA 224
Cdd:pfam01791  77 DCVASVEEAKAMGADAVKVVVYYrvdGSEEEQQMLDEIGRVKEDCHEWGMPLILEGYLRGEAIKDEK-----DPDLVADA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   225 NHLAATIGADIVKQKMAENNGgykaiNYGYTDDRVYSKLTSENPIDLVryqlancymgraglINSGGAagGETDLSDAVR 304
Cdd:pfam01791 152 ARLGAELGADIVKVSYPKNMK-----NAGEEDADVFKRVIKAAPVPYV--------------VLAGGV--SEEDFLRTVR 210
                         250       260
                  ....*....|....*....|..
gi 38704050   305 TAVInkRAGGMGLILGRKAFKK 326
Cdd:pfam01791 211 DAMI--EAGAMGVSSGRNIFQK 230
 
Name Accession Description Interval E-value
PRK09250 PRK09250
class I fructose-bisphosphate aldolase;
1-350 0e+00

class I fructose-bisphosphate aldolase;


Pssm-ID: 236431  Cd Length: 348  Bit Score: 673.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050    1 MTDIAQLLGKDADNLLQHRCmTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHS 80
Cdd:PRK09250   1 MTDIAMLLGKDADSLLSHRC-KIPKDQLHLPGPDFVDRVMIYSDRNPGVLRNLQRLLNHGRLAGTGYLSILPVDQGFEHS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   81 AGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMG 160
Cdd:PRK09250  80 AGASFAPNPLYFDPENIVKLAIEAGCNAVASTLGVLEAVARKYAHKIPFILKLNHNELLSYPNTYDQALTASVEDALRLG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  161 AVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGvDYHVSADLTGQANHLAATIGADIVKQKM 240
Cdd:PRK09250 160 AVAVGATIYFGSEESRRQIEEISEAFEEAHELGLATVLWSYLRNSAFKKDG-DYHTAADLTGQANHLAATIGADIIKQKL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  241 AENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILG 320
Cdd:PRK09250 239 PTNNGGYKAINFGKTDDRVYSKLTSDHPIDLVRYQVANCYMGRRGLINSGGASKGEDDLLDAVRTAVINKRAGGMGLIIG 318
                        330       340       350
                 ....*....|....*....|....*....|
gi 38704050  321 RKAFKKSMADGVKLINAVQDVYLDSKITIA 350
Cdd:PRK09250 319 RKAFQRPMAEGVKLLNAIQDVYLDKKITIA 348
FbaB COG1830
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
48-344 1.18e-94

Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441435 [Multi-domain]  Cd Length: 259  Bit Score: 282.01  E-value: 1.18e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  48 AVLRNMQTLYNtgrlAGTGYLSILPVDQGVEHSAgasfaaNPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRI 127
Cdd:COG1830   3 GKKIRLSRIFN----AGTGRLVIVAVDHGVEHGP------NPGLEDPEEIVRLAAEGGADAVALTKGILERLARKYARDI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 128 PFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAF 207
Cdd:COG1830  73 PLILKLNGSTSLGYPDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPYPRGPAV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 208 KKDGvdyhvSADLTGQANHLAATIGADIVKQKmaennggykainygYTDDrvyskltsenpIDLVRYQLANCYMgraGLI 287
Cdd:COG1830 153 KDET-----DPDLVAHAARIAAELGADIVKTK--------------YPGD-----------PESFREVVAACPV---PVV 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 38704050 288 NSGGA-AGGETDLSDAVRTAVinkRAGGMGLILGRKAFKKSMADGVklINAVQDVYLD 344
Cdd:COG1830 200 IAGGPkTPDDEDFLEMVRDAI---DAGAAGVAVGRNIFQRPNPEAM--LRAISAIVHE 252
DhnA cd00958
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
68-343 4.44e-92

Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.


Pssm-ID: 188645 [Multi-domain]  Cd Length: 235  Bit Score: 274.86  E-value: 4.44e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  68 LSILPVDQGVEHSagasFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQ 147
Cdd:cd00958   1 LVILAVDHGIEHG----FGPNPGLEDPEETVKLAAEGGADAVALTKGIARAYGREYAGDIPLIVKLNGSTSLSPKDDNDK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 148 TLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKdgvdyHVSADLTGQANHL 227
Cdd:cd00958  77 VLVASVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVKN-----EKDPDLIAYAARI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 228 AATIGADIVKQKMAENNGGYKAINYGYTddrvyskltsenpidlvryqlancymgrAGLINSGGAagGETDLSDAVRTAV 307
Cdd:cd00958 152 GAELGADIVKTKYTGDAESFKEVVEGCP----------------------------VPVVIAGGP--KKDSEEEFLKMVY 201
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 38704050 308 INKRAGGMGLILGRKAFKKSmaDGVKLINAVQDVYL 343
Cdd:cd00958 202 DAMEAGAAGVAVGRNIFQRP--DPVAMLRAISAVVH 235
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
68-326 4.04e-78

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 239.21  E-value: 4.04e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050    68 LSILPVDQGVEHSAGASFAanplYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQ 147
Cdd:pfam01791   1 TSILAMDQGVANGPDFAFA----LEDPKVLVAEAATPGANAVLLDPGFIARAHRGYGKDIGLIVALNHGTDLIPINGRDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   148 TLYASVEQAFNMGAVAVGATIYF---GSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGvdyhvSADLTGQA 224
Cdd:pfam01791  77 DCVASVEEAKAMGADAVKVVVYYrvdGSEEEQQMLDEIGRVKEDCHEWGMPLILEGYLRGEAIKDEK-----DPDLVADA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   225 NHLAATIGADIVKQKMAENNGgykaiNYGYTDDRVYSKLTSENPIDLVryqlancymgraglINSGGAagGETDLSDAVR 304
Cdd:pfam01791 152 ARLGAELGADIVKVSYPKNMK-----NAGEEDADVFKRVIKAAPVPYV--------------VLAGGV--SEEDFLRTVR 210
                         250       260
                  ....*....|....*....|..
gi 38704050   305 TAVInkRAGGMGLILGRKAFKK 326
Cdd:pfam01791 211 DAMI--EAGAMGVSSGRNIFQK 230
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
70-320 4.66e-26

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 103.18  E-value: 4.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  70 ILPVDQGVEHsagasfaanplYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAH-RIPFLVKLNHNETLsypnTYDQT 148
Cdd:cd00945   2 DLTLLHPDAT-----------LEDIAKLCDEAIEYGFAAVCVNPGYVRLAADALAGsDVPVIVVVGFPTGL----TTTEV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 149 LYASVEQAFNMGAVAVGATIYFGSEES---RRQIEEISAAFERAhELGMVTVLWAYLRnsafkkdgvdYHVSADLTGQAN 225
Cdd:cd00945  67 KVAEVEEAIDLGADEIDVVINIGSLKEgdwEEVLEEIAAVVEAA-DGGLPLKVILETR----------GLKTADEIAKAA 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050 226 HLAATIGADIVKQKMAENNGGykainygytddrvyskltsENPIDLVRYQLAncYMGRAGLINSGGAAggetdlsdAVRT 305
Cdd:cd00945 136 RIAAEAGADFIKTSTGFGGGG-------------------ATVEDVKLMKEA--VGGRVGVKAAGGIK--------TLED 186
                       250
                ....*....|....*
gi 38704050 306 AVINKRAGGMGLILG 320
Cdd:cd00945 187 ALAAIEAGADGIGTS 201
PRK06852 PRK06852
aldolase; Validated
64-346 2.65e-19

aldolase; Validated


Pssm-ID: 180731  Cd Length: 304  Bit Score: 86.97  E-value: 2.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   64 GTGYLSILPVDQGVEHsagasfaANPLYF---------DPKNIVELAIEAGCNCVASTYGVLAsvsrRYAH---RIPFLV 131
Cdd:PRK06852  29 GTGRLMLFAGDQKIEH-------LNDDFYgegiakddaDPEHLFRIASKAKIGVFATQLGLIA----RYGMdypDVPYLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  132 KLNHNETLSYPNTYD--QTLYASVEQAFNM------GAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLR 203
Cdd:PRK06852  98 KLNSKTNLVKTSQRDplSRQLLDVEQVVEFkensglNILGVGYTIYLGSEYESEMLSEAAQIIYEAHKHGLIAVLWIYPR 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  204 NSAFkKDGVDYHVSADLTGqanhLAATIGADIVKqkmaennggykaINYGYTDdrvyskltSENPIDLVRYQLANCymGR 283
Cdd:PRK06852 178 GKAV-KDEKDPHLIAGAAG----VAACLGADFVK------------VNYPKKE--------GANPAELFKEAVLAA--GR 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38704050  284 AGLINSGGAAGGETD----LSDAVRTavinkrAGGMGLILGRKAFKKSMADGVKLINAVQDVYLDSK 346
Cdd:PRK06852 231 TKVVCAGGSSTDPEEflkqLYEQIHI------SGASGNATGRNIHQKPLDEAVRMCNAIYAITVEDK 291
PRK07226 PRK07226
fructose-bisphosphate aldolase; Provisional
70-341 1.37e-17

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 235973 [Multi-domain]  Cd Length: 267  Bit Score: 81.39  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050   70 ILPVDQGVEHSAGASfaanplYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSyPNTYDQTL 149
Cdd:PRK07226  23 IVPMDHGVSHGPIDG------LVDIRDTVNKVAEGGADAVLMHKGLARHGHRGYGRDVGLIVHLSASTSLS-PDPNDKVL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  150 YASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFkKDGVDYhvsaDLTGQANHLAA 229
Cdd:PRK07226  96 VGTVEEAIKLGADAVSVHVNVGSETEAEMLEDLGEVAEECEEWGMPLLAMMYPRGPGI-KNEYDP----EVVAHAARVAA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  230 TIGADIVKQkmaennggykainyGYTDDR-VYSKLTSENPIDLVryqlancymgraglInSGGA-AGGETDLSDAVRTAV 307
Cdd:PRK07226 171 ELGADIVKT--------------NYTGDPeSFREVVEGCPVPVV--------------I-AGGPkTDTDREFLEMVRDAM 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 38704050  308 inkRAGGMGLILGRKAFKKsmADGVKLINAVQDV 341
Cdd:PRK07226 222 ---EAGAAGVAVGRNVFQH--EDPEAITRAISAV 250
PRK08227 PRK08227
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;
146-237 6.08e-04

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;


Pssm-ID: 181306 [Multi-domain]  Cd Length: 264  Bit Score: 40.79  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38704050  146 DQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTvlwayLRNSAFKKDGVDyhvSADLTGQAN 225
Cdd:PRK08227  93 NEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYGMPV-----MAVTAVGKDMVR---DARYFSLAT 164
                         90
                 ....*....|..
gi 38704050  226 HLAATIGADIVK 237
Cdd:PRK08227 165 RIAAEMGAQIIK 176
 
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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